25b9_cacf
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary formation of ionic salt bridges by charged side chains quaternary arrangement of many protein domains primary sequence of amino acids residues in the protein chain secondary peptide bonds restricting rotation of the backbone MAT25b9_b46a
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary linear sequence of amino acids joined by peptide bonds tertiary ionic salt bridge formations between charged side chains quaternary arrangement of many protein domains secondary backbone hydrogen bonding in α-helices MAT25b9_da16
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary assembly of multiple polypeptide chains into a protein complex secondary φ and ψ dihedral angles tertiary hydrophobic side chain van der Waals (VDW) interactions primary N-terminal to C-terminal list of amino acids MAT25b9_9675
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary van der Waals (VDW) interactions between uncharged side chains secondary hydrogen bonding between nearby backbone atoms in a β-sheet quaternary way in which the different protein subunits are packed together primary order of the amino acids in a polypeptide chain MAT25b9_0058
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary way in which the different protein subunits are packed together primary intramolecular peptide bonds of the linear amino acid chain tertiary van der Waals (VDW) interactions between uncharged side chains secondary β-strand locations within polypeptide backbone MAT25b9_8d35
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary linear sequence of amino acids joined by peptide bonds tertiary hydrophobic side chain interactions quaternary way in which the different protein subunits are packed together secondary β-strand locations within polypeptide backbone MAT25b9_0b97
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary way in which the different protein subunits are packed together tertiary hydrophobic interactions of amino acid side chains secondary backbone hydrogen bonding in α-helices primary intramolecular peptide bonds of the linear amino acid chain MAT25b9_9819
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary N-terminal to C-terminal list of amino acids tertiary hydrophobic interactions of amino acid side chains secondary peptide bonds restricting rotation of the backbone quaternary arrangement of many protein domains MAT25b9_efab
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary manner in which protein subunits are arranged in the native protein tertiary side chains with opposite charges forming ionic bonds primary length of the amino acid chain secondary hydrogen bonding between nearby backbone atoms in a β-sheet MAT25b9_e6d3
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary amino acid sequence in a polypeptide chain secondary formation of a β-strand within the polypeptide backbone tertiary charged side chain interactions quaternary arrangement of subunits into a protein complex MAT25b9_8ed4
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary organization and quantity of folded polypeptide chains secondary α-helix structures linked by backbone hydrogen bonding primary linear sequence of amino acids joined by peptide bonds tertiary hydrophobic side chain interactions MAT25b9_aed2
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary manner in which protein subunits are arranged in the native protein tertiary ionic bonds between oppositely charged side chains primary N-terminal to C-terminal list of amino acids secondary hydrogen bonding between nearby backbone atoms in a β-sheet MAT25b9_e96a
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary hydrophobic side chain interactions primary order of the amino acids in a polypeptide chain quaternary dimers, trimers, tetramers, and pentamers secondary Ramachandran plot of dihedral angles MAT25b9_12ac
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary hydrogen bonding between nearby backbone atoms in a β-sheet primary linear arrangement of the amino acids connected by the peptide bonds quaternary association of two or more polypeptide chains tertiary hydrogen bonding between distant side chain amino acids MAT25b9_e4a9
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary locations of α-helix structures within the backbone tertiary disulfide bridges linking distant amino acids in the same polypeptide chain primary length of the amino acid chain quaternary way in which the different protein subunits are packed together MAT25b9_8721
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary linear arrangement of the amino acids connected by the peptide bonds quaternary dimers, trimers, tetramers, and pentamers tertiary side chain hydrogen bonding between distant amino acids secondary relative orientation of neighboring amino acids MAT25b9_2515
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary hydrogen bonding between nearby backbone atoms in a β-sheet primary formation of peptide bonds to make a polypeptide chain quaternary number and arrangement of multiple folded protein subunits tertiary distant amino acids linked by disulfide bonds MAT25b9_cd60
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary association of two or more polypeptide chains tertiary side chain hydrogen bonding between distant amino acids primary linear arrangement of the amino acids connected by the peptide bonds secondary formation of a β-strand within the polypeptide backbone MAT25b9_6225
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary intramolecular peptide bonds of the linear amino acid chain secondary Ramachandran plot of dihedral angles tertiary distant amino acids linked by disulfide bonds quaternary homo- and hetero-oligomers MAT25b9_8a2d
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary formation of peptide bonds to make a polypeptide chain secondary peptide bonds restricting rotation of the backbone tertiary hydrophobic interactions of amino acid side chains quaternary arrangement of subunits into a protein complex MAT25b9_d10d
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary order of the amino acids in a polypeptide chain tertiary three-dimensional shape of a single polypeptide chain secondary α-helix structures linked by backbone hydrogen bonding quaternary formation of oligomers from two or more protein subunits MAT25b9_657e
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary organization and quantity of folded polypeptide chains secondary formation of a α-helix within the polypeptide backbone tertiary formation of disulfide bonds by special side chains primary N-terminal to C-terminal list of amino acids MAT25b9_2b25
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary charged side chain interactions quaternary formation of oligomers from two or more protein subunits primary length of the amino acid chain secondary angular orientation between adjacent amino acids MAT25b9_87cc
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary ionic salt bridge formations between charged side chains quaternary homo- and hetero-oligomers secondary hydrogen bonding between nearby backbone atoms in a β-sheet primary linear arrangement of the amino acids connected by the peptide bonds MAT25b9_d957
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary order of the amino acids in a polypeptide chain tertiary side chain hydrogen bonding between distant amino acids quaternary manner in which protein subunits are arranged in the native protein secondary formation of a β-strand within the polypeptide backbone MAT25b9_2a4c
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary intramolecular peptide bonds of the linear amino acid chain quaternary assembly of multiple polypeptide chains into a protein complex secondary relative orientation of neighboring amino acids tertiary hydrophobic side chain van der Waals (VDW) interactions MAT25b9_dd77
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary number and arrangement of multiple folded protein subunits tertiary creation of disulfide bridges by specific side chains primary amino acid sequence in a polypeptide chain secondary peptide bonds restricting rotation of the backbone MAT25b9_17a4
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary locations of α-helix structures within the backbone primary N-terminal to C-terminal list of amino acids tertiary creation of hydrophobic core quaternary homo- and hetero-oligomers MAT25b9_4530
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary arrangement of subunits into a protein complex primary intramolecular peptide bonds of the linear amino acid chain tertiary formation of disulfide bonds by special side chains secondary formation of a α-helix within the polypeptide backbone MAT25b9_7605
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary ionic bonds between oppositely charged side chains primary amino acid sequence in a polypeptide chain secondary formation of a α-helix within the polypeptide backbone quaternary manner in which protein subunits are arranged in the native protein MAT25b9_6bc3
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary assembly of multiple polypeptide chains into a protein complex primary linear arrangement of the amino acids connected by the peptide bonds tertiary three-dimensional shape of a single polypeptide chain secondary locations of α-helix structures within the backbone MAT25b9_b8f2
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary association of two or more polypeptide chains primary linear sequence of amino acids joined by peptide bonds tertiary charged side chain interactions secondary backbone dihedral angles MAT25b9_24d8
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary complete three-dimensional conformation quaternary manner in which protein subunits are arranged in the native protein secondary hydrogen bonding between nearby backbone atoms in a β-sheet primary sequence of amino acids residues in the protein chain MAT25b9_f066
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary intramolecular peptide bonds of the linear amino acid chain quaternary way in which the different protein subunits are packed together tertiary complete three-dimensional conformation secondary peptide bonds restricting rotation of the backbone MAT25b9_598a
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary relative orientation of one protein subunits to another protein subunit primary linear arrangement of the amino acids connected by the peptide bonds tertiary creation of hydrophobic core secondary backbone dihedral angles MAT25b9_3e0f
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary N-terminal to C-terminal list of amino acids tertiary van der Waals (VDW) interactions between uncharged side chains secondary backbone hydrogen bonding in α-helices quaternary association of two or more polypeptide chains MAT25b9_5229
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary organization and quantity of folded polypeptide chains tertiary three-dimensional shape of a single polypeptide chain primary order of the amino acids in a polypeptide chain secondary formation of a β-strand within the polypeptide backbone MAT25b9_d688
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary N-terminal to C-terminal list of amino acids quaternary assembly of multiple polypeptide chains into a protein complex tertiary complete three-dimensional conformation secondary relative orientation of neighboring amino acids MAT25b9_200c
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary formation of disulfide bonds by special side chains quaternary formation of oligomers from two or more protein subunits primary formation of peptide bonds to make a polypeptide chain secondary α-helix structures linked by backbone hydrogen bonding MAT25b9_48f7
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary arrangement of subunits into a protein complex primary sequence of amino acids residues in the protein chain secondary formation of a β-strand within the polypeptide backbone tertiary distant amino acids linked by disulfide bonds MAT25b9_2375
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary relative orientation of neighboring amino acids quaternary formation of oligomers from two or more protein subunits primary order of the amino acids in a polypeptide chain tertiary distant amino acids linked by disulfide bonds MAT25b9_87c2
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary peptide bonds forming a linear chain of amino acids tertiary complete three-dimensional conformation quaternary relative orientation of one protein subunits to another protein subunit secondary angular orientation between adjacent amino acids MAT25b9_7f06
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary locations of α-helix structures within the backbone primary length of the amino acid chain tertiary hydrogen bonding between polar side chains quaternary organization and quantity of folded polypeptide chains MAT25b9_0e4c
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary hydrogen bonding between nearby backbone atoms in a β-sheet tertiary hydrogen bonding between polar side chains primary linear arrangement of the amino acids connected by the peptide bonds quaternary number and arrangement of multiple folded protein subunits MAT25b9_fc99
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary amino acid chain length tertiary electrostatic interactions among charged side chains quaternary homo- and hetero-oligomers secondary β-strand locations within polypeptide backbone MAT25b9_f89b
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary disulfide bridges linking distant amino acids in the same polypeptide chain secondary hydrogen bonding between nearby backbone atoms in a β-sheet quaternary arrangement of many protein domains primary sequence of amino acids residues in the protein chain MAT25b9_b1e7
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary β-strand locations within polypeptide backbone quaternary dimers, trimers, tetramers, and pentamers tertiary formation of ionic salt bridges by charged side chains primary intramolecular peptide bonds of the linear amino acid chain MAT25b9_9f50
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary hydrophobic side chain van der Waals (VDW) interactions primary linear sequence of amino acids joined by peptide bonds secondary formation of a α-helix within the polypeptide backbone quaternary manner in which protein subunits are arranged in the native protein MAT25b9_90cf
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary number and arrangement of multiple folded protein subunits primary intramolecular peptide bonds of the linear amino acid chain tertiary side chain hydrogen bonding between distant amino acids secondary peptide bonds restricting rotation of the backbone MAT25b9_2da4
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary way in which the different protein subunits are packed together primary formation of peptide bonds to make a polypeptide chain tertiary hydrophobic interactions of amino acid side chains secondary Ramachandran plot of dihedral angles MAT25b9_2b6c
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary linear arrangement of the amino acids connected by the peptide bonds tertiary highest level for a protein with a single peptide chain secondary β-strand locations within polypeptide backbone quaternary homo- and hetero-oligomers MAT25b9_3a39
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary peptide bonds restricting rotation of the backbone primary peptide bonds forming a linear chain of amino acids quaternary assembly of multiple polypeptide chains into a protein complex tertiary hydrogen bonding between polar side chains MAT25b9_3f40
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary hydrophobic interactions of amino acid side chains secondary Ramachandran plot of dihedral angles quaternary relative orientation of one protein subunits to another protein subunit primary sequence of amino acids residues in the protein chain MAT25b9_5427
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary creation of disulfide bridges by specific side chains secondary relative orientation of neighboring amino acids primary sequence of amino acids residues in the protein chain quaternary arrangement of subunits into a protein complex MAT25b9_f07c
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary arrangement of subunits into a protein complex secondary backbone hydrogen bonding in α-helices tertiary hydrophobic interactions of amino acid side chains primary peptide bonds forming a linear chain of amino acids MAT25b9_f6b9
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary electrostatic interactions among charged side chains secondary formation of a α-helix within the polypeptide backbone quaternary relative orientation of one protein subunits to another protein subunit primary intramolecular peptide bonds of the linear amino acid chain MAT25b9_b007
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary Ramachandran plot of dihedral angles primary amino acid chain length quaternary relative orientation of one protein subunits to another protein subunit tertiary hydrogen bonding between distant side chain amino acids MAT25b9_7c60
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary angular orientation between adjacent amino acids primary formation of peptide bonds to make a polypeptide chain quaternary arrangement of many protein domains tertiary hydrophobic side chain interactions MAT25b9_52b4
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary arrangement of subunits into a protein complex tertiary formation of ionic salt bridges by charged side chains primary linear sequence of amino acids joined by peptide bonds secondary φ and ψ dihedral angles MAT25b9_55d6
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary order of the amino acids in a polypeptide chain secondary α-helix structures linked by backbone hydrogen bonding quaternary manner in which protein subunits are arranged in the native protein tertiary distant amino acids linked by disulfide bonds MAT25b9_26b8
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary β-strand locations within polypeptide backbone quaternary arrangement of subunits into a protein complex primary peptide bonds forming a linear chain of amino acids tertiary electrostatic interactions among charged side chains MAT25b9_a043
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary side chain hydrogen bonding between distant amino acids quaternary arrangement of many protein domains secondary relative orientation of neighboring amino acids primary amino acid chain length MAT25b9_2cf4
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary distant amino acids linked by disulfide bonds primary intramolecular peptide bonds of the linear amino acid chain secondary φ and ψ dihedral angles quaternary arrangement of many protein domains MAT25b9_3089
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary distant amino acids linked by disulfide bonds secondary φ and ψ dihedral angles primary formation of peptide bonds to make a polypeptide chain quaternary association of two or more polypeptide chains MAT25b9_2b98
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary hydrophobic side chain van der Waals (VDW) interactions quaternary relative orientation of one protein subunits to another protein subunit primary peptide bonds forming a linear chain of amino acids secondary relative orientation of neighboring amino acids MAT25b9_b4f8
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary linear sequence of amino acids joined by peptide bonds secondary hydrogen bonding between nearby backbone atoms in the polypeptide chain tertiary van der Waals (VDW) interactions between uncharged side chains quaternary association of two or more polypeptide chains MAT25b9_ebd7
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary highest level for a protein with a single peptide chain secondary β-strand locations within polypeptide backbone quaternary dimers, trimers, tetramers, and pentamers primary linear sequence of amino acids joined by peptide bonds MAT25b9_4c5d
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary way in which the different protein subunits are packed together secondary restriction of backbone rotation by peptide bonds primary amino acid chain length tertiary hydrophobic interactions of amino acid side chains MAT25b9_41f8
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary linear sequence of amino acids joined by peptide bonds quaternary arrangement of subunits into a protein complex secondary peptide bonds restricting rotation of the backbone tertiary formation of ionic salt bridges by charged side chains MAT25b9_182f
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary assembly of multiple polypeptide chains into a protein complex primary intramolecular peptide bonds of the linear amino acid chain tertiary hydrogen bonding between polar side chains secondary formation of a α-helix within the polypeptide backbone MAT25b9_f5a3
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary φ and ψ dihedral angles primary length of the amino acid chain tertiary side chain hydrogen bonding between distant amino acids quaternary formation of oligomers from two or more protein subunits MAT25b9_fc57
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary backbone dihedral angles tertiary creation of hydrophobic core primary sequence of amino acids residues in the protein chain quaternary dimers, trimers, tetramers, and pentamers MAT25b9_859e
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary dimers, trimers, tetramers, and pentamers secondary relative orientation of neighboring amino acids primary length of the amino acid chain tertiary highest level for a protein with a single peptide chain MAT25b9_fc94
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary N-terminal to C-terminal list of amino acids secondary Ramachandran plot of dihedral angles quaternary manner in which protein subunits are arranged in the native protein tertiary van der Waals (VDW) interactions between uncharged side chains MAT25b9_1677
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary formation of peptide bonds to make a polypeptide chain tertiary ionic salt bridge formations between charged side chains secondary angular orientation between adjacent amino acids quaternary arrangement of subunits into a protein complex MAT25b9_24ae
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary sequence of amino acids residues in the protein chain quaternary dimers, trimers, tetramers, and pentamers secondary relative orientation of neighboring amino acids tertiary creation of disulfide bridges by specific side chains MAT25b9_e572
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary highest level for a protein with a single peptide chain primary order of the amino acids in a polypeptide chain secondary hydrogen bonding between nearby backbone atoms in a β-sheet quaternary association of two or more polypeptide chains MAT25b9_9fe6
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary complete three-dimensional conformation secondary angular orientation between adjacent amino acids quaternary association of two or more polypeptide chains primary order of the amino acids in a polypeptide chain MAT25b9_290b
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary association of two or more polypeptide chains primary intramolecular peptide bonds of the linear amino acid chain secondary φ and ψ dihedral angles tertiary hydrophobic interactions of amino acid side chains MAT25b9_cda4
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary formation of peptide bonds to make a polypeptide chain quaternary dimers, trimers, tetramers, and pentamers secondary formation of a β-strand within the polypeptide backbone tertiary complete three-dimensional conformation MAT25b9_d46a
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary hydrogen bonding between nearby backbone atoms in the polypeptide chain primary amino acid chain length tertiary hydrophobic side chain interactions quaternary way in which the different protein subunits are packed together MAT25b9_ab97
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary association of two or more polypeptide chains tertiary complete three-dimensional conformation secondary β-strand locations within polypeptide backbone primary sequence of amino acids residues in the protein chain MAT25b9_606d
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary formation of oligomers from two or more protein subunits tertiary distant amino acids linked by disulfide bonds primary N-terminal to C-terminal list of amino acids secondary hydrogen bonding between nearby backbone atoms in the polypeptide chain MAT25b9_20aa
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary homo- and hetero-oligomers tertiary hydrogen bonding between distant side chain amino acids secondary peptide bonds restricting rotation of the backbone primary amino acid chain length MAT25b9_8bc6
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary formation of peptide bonds to make a polypeptide chain tertiary creation of disulfide bridges by specific side chains secondary restriction of backbone rotation by peptide bonds quaternary homo- and hetero-oligomers MAT25b9_e939
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
secondary locations of α-helix structures within the backbone tertiary ionic bonds between oppositely charged side chains primary N-terminal to C-terminal list of amino acids quaternary number and arrangement of multiple folded protein subunits MAT25b9_f0c3
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary dimers, trimers, tetramers, and pentamers secondary backbone hydrogen bonding in α-helices tertiary hydrophobic side chain van der Waals (VDW) interactions primary length of the amino acid chain MAT25b9_1167
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary organization and quantity of folded polypeptide chains primary peptide bonds forming a linear chain of amino acids secondary φ and ψ dihedral angles tertiary ionic bonds between oppositely charged side chains MAT25b9_d930
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary linear sequence of amino acids joined by peptide bonds secondary Ramachandran plot of dihedral angles tertiary hydrogen bonding between polar side chains quaternary arrangement of subunits into a protein complex MAT25b9_f6b7
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary number and arrangement of multiple folded protein subunits tertiary side chains with opposite charges forming ionic bonds secondary backbone hydrogen bonding in α-helices primary N-terminal to C-terminal list of amino acids MAT25b9_b1a9
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary formation of oligomers from two or more protein subunits secondary restriction of backbone rotation by peptide bonds tertiary charged side chain interactions primary length of the amino acid chain MAT25b9_0489
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary intramolecular peptide bonds of the linear amino acid chain quaternary association of two or more polypeptide chains secondary relative orientation of neighboring amino acids tertiary three-dimensional shape of a single polypeptide chain MAT25b9_c80d
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary ionic bonds between oppositely charged side chains quaternary assembly of multiple polypeptide chains into a protein complex primary linear arrangement of the amino acids connected by the peptide bonds secondary locations of α-helix structures within the backbone MAT25b9_aaa3
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary ionic salt bridge formations between charged side chains secondary β-strand locations within polypeptide backbone primary amino acid chain length quaternary assembly of multiple polypeptide chains into a protein complex MAT25b9_fe90
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary electrostatic interactions among charged side chains secondary backbone hydrogen bonding in α-helices quaternary homo- and hetero-oligomers primary formation of peptide bonds to make a polypeptide chain MAT25b9_98cc
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary complete three-dimensional conformation quaternary arrangement of many protein domains secondary backbone dihedral angles primary order of the amino acids in a polypeptide chain MAT25b9_ff40
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
tertiary three-dimensional shape of a single polypeptide chain quaternary homo- and hetero-oligomers primary formation of peptide bonds to make a polypeptide chain secondary backbone hydrogen bonding in α-helices MAT25b9_7037
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
primary amino acid chain length quaternary way in which the different protein subunits are packed together tertiary charged side chain interactions secondary α-helix structures linked by backbone hydrogen bonding MAT25b9_7b6d
Match each of the following levels of protein structure with their corresponding descriptions.
Note: Each choice will be used exactly once.
quaternary arrangement of subunits into a protein complex tertiary side chains with opposite charges forming ionic bonds secondary α-helix structures linked by backbone hydrogen bonding primary formation of peptide bonds to make a polypeptide chain