Protein Structure - TRQ Flashcards

1
Q

Dense hydrophobic cores are typical of…

A

Globular protein

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2
Q

Collagen is found in a(n)…

A

triple helix

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3
Q

Peptide bonds have a structure and geometry which is …

A

Rigid and planar

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4
Q

Secondary structure is stabilized by …

A

Hydrogen bonds

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5
Q

Silk fibroin is found in a(n) …

A

beta conformation

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6
Q

Beta-turns link together two adjacent segments of …

A

Antiparallel beta sheets

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7
Q

A recognizable folding pattern involving two or more elements of secondary structure is called…

A

Motif

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8
Q

a loss of 3-D structure sufficient to cause loss of function is called …

A

denaturation

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9
Q

A part of a polypeptide chain that is independently stable or could undergo movements as a single entity is known as a …

A

Domain

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10
Q

A visual description of the combinations of dihedral angles that are permitted in a peptide backbone is called …

A

Ramachandran plot

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11
Q

An example of a family of chaperones is …

A

Hsp70

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12
Q

An idealized alpha-helix contains how many residues per turn?

A

3.6 residues/turn

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13
Q

Biochemists can estimate the fraction of protein made up of a helix or beta sheet using …

A

Circular dichroism (CD) spectroscopy

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14
Q

In the beta conformation of polypeptide chains, the backbone is extended into a …

A

Zigzag

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15
Q

In alpha-keratins, the cross-links stabilizing quaternary structure are …

A

Disulfide bonds

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16
Q

Most enzymes and regulatory proteins are …

A

Globular proteins

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17
Q

Proteins can be denatured by …

A

Heat and extremes of pH

18
Q

Proteins in their functional, folded conformations are called …

A

Native proteins

19
Q

Proteins that catalyze the accurate folding of proteins are called …

A

Chaperones

20
Q

Proteins with polypeptide chains folded into a spherical or globular shape are called …

A

Globular proteins

21
Q

Proteins with polypeptide chains arranged in long strands or sheets are called …

A

Fibrous proteins

22
Q

Proteins with significant similarity primary structure and/or tertiary structure and function are said to be in the same …

A

protein family

23
Q

Returning to conditions in which the native conformation is stable is called …

A

Renaturation

24
Q

Since the loss of structure in one part of the protein destabilizes other parts, the process of unfolding is …

A

Cooperative

25
Q

Some multimeric proteins have a repeated unit consisting of a singe subunit or group of subunits called …

A

Protomer

26
Q

The C-N bond in a peptide group cannot rotate freely because of …

A

Partial double-bond characters

27
Q

The coiled-coil motif is found in …

A

alpha-Keratin

28
Q

The local spatial arrangement of polypeptides is called …

A

Secondary structure

29
Q

The spatial arrangement of atoms in a protein or any part of a protein is called its …

A

Conformation

30
Q

The arrangement of two or more separate polypeptide chains in 3-D complexes is termed …

A

Quaternary structure

31
Q

The elements that connect segments of antiparallel beta sheets are called …

A

beta turns

32
Q

The major contributor in stabilizing the globular form of most soluble proteins is …

A

Hydrophobic interactions

33
Q

The overall 3-D arrangement of all atoms in a protein, including longer-range aspects of amino acid sequence, is termed …

A

Tertiary structure

34
Q

The structures that provide support, shape, and external protection to vertebrates are made of …

A

fibrous proteins

35
Q

These proteins constitute hair, nails, wools, and much of the outer layer of skin.

A

alpha-keratin

36
Q

This enzyme catalyzes the interchange of disulfide bonds until the native conformation is formed.

A

Protein disulfide isomerase (PDI)

37
Q

This enzyme catalyzes the interconversion of the cis and trans isomers of Pro residue peptide bonds.

A

Peptide prolyl cis-trans isomerase (PPI)

38
Q

This protein structure is found int he beta conformation and has soft, flexible filaments.

A

silk fibroin

39
Q

This type of protein is found in connective tissue , such as tendon or cartilage.

A

collagen

40
Q
A