AMINO ACIDS Flashcards

1
Q

are the most abundant and functionally diverse molecules in living systems.

A

Proteins

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2
Q

direct and regulate metabolism in the body, whereas contractile proteins in muscle permit movement.

A

Enzymes and polypeptide hormones:

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3
Q

have a carboxyl group, a primary amino group (except for proline, which has a secondary amino group), and a distinctive side chain (“R group”) bonded to the α-carbon atom

A

Amino Acids

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4
Q

is the result of the hydrophobicity of the nonpolar R groups, which act much like droplets of oil that coalesce in an aqueous environment.

A

hydrophobic effect

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5
Q

its side chain and α-amino N form a rigid, five-membered ring structure.
has a secondary (rather than a primary) amino group.
It is frequently referred to as an “imino acid.”

A

Proline

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6
Q

Two disulfide-linked cysteines are referred to as

A

cystine

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7
Q

is the only amino acid with a side chain that can ionize within the physiologic pH range.

A

Histidine

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8
Q

is a solution that resists change in pH following the addition of an acid or base.

A

Buffers

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9
Q

is the linear sequence of amino acids in a protein. It is determined by the DNA sequence of the gene that codes for the protein.

A

PRIMARY STRUCTURE OF PROTEINS

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10
Q

is the formation of regular arrangements of amino acids that are located near each other in the linear sequence.

A

SECONDARY STRUCTURE OF PROTEINS

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11
Q

-the most common of the helices
spiral structure, tightly packed, coiled polypeptide backbone core, with the side chains of the component amino acids

A

a-Helix

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12
Q

–surfaces of β-sheets appear “pleated”
β-strands are often visualized as broad arrows

A

β-Sheet

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13
Q

reverse the direction of a polypeptide chain, helping it form a compact, globular shape.

A

β-Bends (reverse turns, β-turns)

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14
Q
  • refers both to the folding of domains (the basic units of structure and function), and to the final arrangement of domains in the polypeptide.
A

TERTIARY STRUCTURE OF GLOBULAR PROTEINS

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15
Q

involves non-random, ordered pathways

A

Protein folding

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16
Q

results in the unfolding and disorganization of a protein’s secondary and tertiary structures without the hydrolysis of peptide bonds.

A

Denaturation of proteins

17
Q

is the three-dimensional arrangement of multiple protein subunits.

A

QUATERNARY STRUCTURE OF PROTEINS

18
Q

accumulation of these insoluble, spontaneously aggregating proteins, called amyloids (Parkinson, Huntington, and Alzheimer disease).

A

Amyloid disease

19
Q
A