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principles of biochem lehninger chapter 4 2024
Entire 3D structure of a single-chain polymer, as a result of side chain interactions. Set up to maximize
favorable interactions and minimize unfavorable interactions. - answer-Tertiary structure
Spatial arrangement of a macromolecule's individual subunits. 3D arrangement of different polypeptides
in an arrangement of subunits and the total nature of their interactions. - answer-Quaternary structure
Bond between two amino acids (carboxylic acid and amino groups). Typically takes on the trans
conformation and is rigid/planar. - answer-Peptide bond
Sequence of amino acids linked by peptide bonds - peptide chains - answer-Primary structure
Local spatial arrangement of a polymer's backbone atoms without side chains. 3D arrangement of parts
of a chain
2 main types: a-helix and β-sheet - answer-Secondary structure
what is secondary structure stabilized by? - answer-H bonds between polar backbone groups
The linking of two AA is accompanied by the loss of what? - answer-A water molecule. Condensation
reaction.
The amino end, or the beginning of a polypeptide chain. - answer-N terminal
The carboxyl end, or the end of a polypeptide chain - answer-C terminal
Regularly repeating part of a polypeptide chain rich in hydrogen bonding potential. Rigid planes
separated by substituted methylene groups - answer-Backbone
what does each amino acid residue contain? - answer-A carbonyl group and an amino group
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good hydrogen bond acceptor - answer-R-C=O
good hydrogen bond donor - answer-R-N-H
Most common kind of cross-links (seen between cysteines) - answer-Disulfide bonds
The _______ structure is the native conformation of a protein. - answer-Tertiary
Tertiary structure is held up by five interaction types of: - answer-1) H-bonds; found w/in alpha-helix,
beta-sheet, & between R groups
2) Hydrophobic interactions
3) Disulfide bridges
4) Electrostatic interactions; between charged groups (ionic ) - salt bridges
5) Prosthetic group; between metal & groups of peptide chain, coordinated covalent bonds
Have a compact/highly folded structure (no H2O molecules or empty spaces inside) and are water
soluble. Perform most chemical transactions in cell. - answer-Globular proteins
Is the inside of a protein polar or non polar? - answer-Nonpolar
Is the outside of a protein polar or non polar? - answer-Polar
What kind of interactions take place among subunits of proteins displaying quaternary structure? -
answer-Weak interactions
Two identical subunits: - answer-Dimer
Proteins with extended structure and low solubility in water: - answer-fibrous proteins
principles of biochem lehninger chapter 4 2024
Entire 3D structure of a single-chain polymer, as a result of side chain interactions. Set up to maximize
favorable interactions and minimize unfavorable interactions. - answer-Tertiary structure
Spatial arrangement of a macromolecule's individual subunits. 3D arrangement of different polypeptides
in an arrangement of subunits and the total nature of their interactions. - answer-Quaternary structure
Bond between two amino acids (carboxylic acid and amino groups). Typically takes on the trans
conformation and is rigid/planar. - answer-Peptide bond
Sequence of amino acids linked by peptide bonds - peptide chains - answer-Primary structure
Local spatial arrangement of a polymer's backbone atoms without side chains. 3D arrangement of parts
of a chain
2 main types: a-helix and β-sheet - answer-Secondary structure
what is secondary structure stabilized by? - answer-H bonds between polar backbone groups
The linking of two AA is accompanied by the loss of what? - answer-A water molecule. Condensation
reaction.
The amino end, or the beginning of a polypeptide chain. - answer-N terminal
The carboxyl end, or the end of a polypeptide chain - answer-C terminal
Regularly repeating part of a polypeptide chain rich in hydrogen bonding potential. Rigid planes
separated by substituted methylene groups - answer-Backbone
what does each amino acid residue contain? - answer-A carbonyl group and an amino group
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good hydrogen bond acceptor - answer-R-C=O
good hydrogen bond donor - answer-R-N-H
Most common kind of cross-links (seen between cysteines) - answer-Disulfide bonds
The _______ structure is the native conformation of a protein. - answer-Tertiary
Tertiary structure is held up by five interaction types of: - answer-1) H-bonds; found w/in alpha-helix,
beta-sheet, & between R groups
2) Hydrophobic interactions
3) Disulfide bridges
4) Electrostatic interactions; between charged groups (ionic ) - salt bridges
5) Prosthetic group; between metal & groups of peptide chain, coordinated covalent bonds
Have a compact/highly folded structure (no H2O molecules or empty spaces inside) and are water
soluble. Perform most chemical transactions in cell. - answer-Globular proteins
Is the inside of a protein polar or non polar? - answer-Nonpolar
Is the outside of a protein polar or non polar? - answer-Polar
What kind of interactions take place among subunits of proteins displaying quaternary structure? -
answer-Weak interactions
Two identical subunits: - answer-Dimer
Proteins with extended structure and low solubility in water: - answer-fibrous proteins
