________: There is an amino group- (NH3 +) on one end of the backbone and a carboxyl group- (Coo)- on the other.
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dimensional shape
A proteins distinctive overall three- ________, or tertiary structure, results from interactions between residues that are brought together as the backbone bends and folds in space.
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Enzyme
A protein that functions as a catalyst is called an
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Flexibility
________: Although the peptide bond itself can not rotate because of its double- bond nature, the single bonds on either side of the peptide bond can rotate.
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Polymers
________ that contain 50 or more amino acids are called polypeptides " (many- peptides)
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Biochemists
________ refer to the unique sequence of amino acids in a protein as its primary structure.
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macromolecular machines
In addition, cells contain ________: complexes of multiple proteins that assemble to carηr out a particular function.
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COOH
________- a carboxyl functional group.
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protein
The ________ is often used to describe any chain of amino acid residues.
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R groups
Both polar and electrically charged ________ interact readily with water and are hydrophilic.
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Cαtαlysis
________ are specialized to catalyze, or speed up, chemical reactions.
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quaternary structure
The combination of polypeptides, referred to as subunits, gives some proteins ________.
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central carbon
In all 20 amino acids, a(n) ________ atom (referred to as the carbon) bonds covalently to four different atoms or groups of atoms:
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Nonpolar R groups
________ lack charged or highly electronegative atoms capable of forming hydrogen bonds with water.
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R group
If the ________ in your amino acid does not have a negative charge, a positive charge, or an oxygen atom, then you are looking at a nonpolar amino acid, such as methionine.
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R group
The ________, or side chain, represents the part of the amino acid core structure that makes each of the 20 different amino acids unique.
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R-group orientαfion
The side chains of each residue extend out from the backbone, making it possible for them to interact with each other and with water
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Directionαnal
There is an amino group (-NH3 +) on one end of the backbone and a carboxyl group (-Coo-) on the other
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Flexibility
Although the peptide bond itself cannot rotate because of its double-bond nature, the single bonds on either side of the peptide bond can rotate
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In addition, cells contain macromolecular machines
complexes of multiple proteins that assemble to carηr out a particular function
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Hydrophilic
Both polar and electrically charged R-groups interact readily with water and are
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Hydrophobic
Nonpolar R-groups lack charged or highly electronegative atoms capable of forming hydrogen bonds with water.
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Peptide bond
The C-N covalent bond that results from this condensation reaction is called
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oligopeptide
Generally, when fewer than 50 amino acids are linked together in this way, the resulting polymer is called an
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Polypeptides
Polymers that contain 50 or more amino acids are called
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Primary structure
Biochemists refer to the unique sequence of amino acids in a protein as its
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Macromolecular machines
complexes of multiple proteins that assemble to carry out a particular function.
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