________ is a secondary protein structure in which a protein chain forms a right- handed coil stabilized by hydrogen bonds between peptide groups along its backbone.
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Residue
________ is an amino acid unit in a polypeptide.
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Alpha amino acid
is an amino acid in which the amino group is bonded to the carbon atom next to the ¬COOH group.
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Organic compounds
________: Polar solvents such as acetone and ethanol interfere with hydrogen bonding by competing for bonding sites.
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insoluble collagen
Cooking meat converts some of the ________ into soluble gelatin, which can be used in glue and for thickening sauces.
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Secondary protein structure
regular and repeating structural patterns created by hydrogen bonding between backbone atoms in neighbouring segments of protein chains.
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Zwitterion
________ is a neutral dipolar ion that has one positive charge and one negative charge.
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bacterial protein
The disinfectant action of ethanol, for example, results from its ability to denature ________.
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→Agents
________ that cause denaturation include heat, mechanical agitation, detergents, organic solvents, extremely acidic or basic pH, and inorganic salts:
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salt bridge
A(n) ________ is a noncovalent bond; it is an ionic bond.
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Mechanical agitation
________: The most familiar example of denaturation by agitation is the foam produced by beating egg whites.
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Biochemistry
________ is the study of molecules and their reactions in living organisms.
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PH change
________: Excess H+ or OH- ions react with the basic or acidic side chains in amino acid residues and disrupt salt bridges.
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Noncovalent forces
________ are forces of attraction other than covalent bonds that can act between molecules or within molecules.
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hydrophobic substance
A(n) ________ does not dissolve in water.
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Detergents
very low concentrations of detergents can cause denaturation by disrupting the association of hydrophobic side chains.
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Amino acids
molecule that contains both an amino functional group and a carboxyl functional group
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amino acid
The pI for each ________ is different, due to the influence of the side- chain functional groups.
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Alpha
amino acid is an amino acid in which the amino group is bonded to the carbon atom next to the ¬COOH group
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Carboxyl-terminal (C-terminal) amino acid is the amino acid with the free ¬COO
group at the end of a protein
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Heat
The weak side-chain attractions in globular proteins are easily disrupted by heating, in many cases only to temperatures above 50 °C (323 K)
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Mechanical agitation
The most familiar example of denaturation by agitation is the foam produced by beating egg whites
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Detergents
Even very low concentrations of detergents can cause denaturation by disrupting the association of hydrophobic side chains
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Organic compounds
Polar solvents such as acetone and ethanol interfere with hydrogen bonding by competing for bonding sites
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Inorganic salts
Sufficiently high concentrations of ions can disturb salt bridges
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quaternary structure
two or more protein chains assembled in a larger three-dimensional structure held together by noncovalent interactions.
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denaturation
the loss of secondary, tertiary, or quaternary protein structure due to disruption of noncovalent interactions and/or disulfide bonds that leaves peptide bonds and primary structure intact.
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Flashcard (21)