Chapter 6 - Key Concepts & Review Points Flashcards

1
Q

The planar character of the peptide bond limits the ____________ of the polypeptide chain.

A

conformational flexibility

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2
Q

The alpha helix and beta sheet allow the polypeptide to adopt favorable ____________.

A

dihedral angles

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3
Q

Fibrous proteins contain long stretches of regular secondary structure, such as the ____________ in alpha keratin and the ____________ in collagen.

A

coiled coils

triple helix

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4
Q

Not all polypeptide segments from regular secondary structure such as ____________ or ____________.

A

alpha helices

beta sheets

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5
Q

X-ray crysallography and NMR spectroscopy are used to determine the positions of ____________ in proteins.

A

atoms

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6
Q

Nonpolar residues tend to occur in the protein ____________ and polar residues on the ____________.

A

interior

exterior

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7
Q

A protein’s tertiary structure consists of secondary structural elements that combine to form ____________ and ____________.

A

motifs

domains

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8
Q

Over time, a protein’s ____________ is more highly conserved than its ____________.

A

structure

sequence

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9
Q

Bioinformatics databases store ____________. Software makes it possible to visualize proteins and compare their structural features.

A

macromolecular structure coordinates

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10
Q

Some proteins contain multiple ____________, usually arranged symmetrically.

A

subunits

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11
Q

Protein stability depends primarily on ____________ and secondarily on ____________.

A

hydrophobic effects

electrostatic interactions

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12
Q

A protein that has been denatured my undergo ____________.

A

renaturation

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13
Q

Protein structures are ____________ and may include unfolded regions.

A

flexible

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14
Q

A folding protein follows a pathway from ________ energy and ________ entropy to ________ energy and ________ entropy.

A

high
high
low
low

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15
Q

Protein disulfide isomerase catalyzes ____________.

A

disulfide bond formation

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16
Q

A variety of molecular chaperones assist protein folding via a(n) ________________ mechanism.

A

ATP-dependent bind-and-release

17
Q

Amyloid diseases result from ____________.

A

protein misfolding

18
Q

The misfolded proteins form fibrils containing extensive ____________.

A

beta structure

19
Q

________ levels of structural complexity are used to describe the three-dimensional shapes of proteins.

A

four

20
Q

The conformational flexibility of the peptide group is described by its ____________.

A

dihedral angles (or phi and psi torsion angles)

21
Q

The alpha helix is a regular secondary structure in which hydrogen bonds form between backbone groups ________ residues apart. In the beta sheet, hydrogen bonds form between ________________.

A

four

backbones of separate polypeptide segments

22
Q

Fibrous proteins are characterized by a single type of ____________ structure: alpha keratin is a ____-handed coil of ________ alpha helices, and collagen is a ____-handed triple helix with ________ residues per turn.

A
secondary
left
two
left
three
23
Q

The structures of proteins have been determined mainly by ____________ and ____________.

A

x-ray crystallography

NMR spectroscopy

24
Q

The nonpolar side chains of a globular protein tend to occupy the protein’s ____________; the polar side chains tend to define its ____________.

A

interior

surface

25
Q

Protein structures can be classified on the basis of ____________, ____________, ____________, or ____________. Structural elements are more likely to be evolutionarily conserved than are amino acid sequences.

A

motifs
secondary structure content
topology
domain architecture

26
Q

Structural bioinformatic is concerned with the ____________, ____________, ____________, and ____________ of macromolecular structures.

A

storage
visualization
analysis
comparison

27
Q

The indiviual subunits of multisubunit proteins are usually ____________ arranged.

A

symmetrically

28
Q

____________ protein structures are only slightly more stable than their ____________ forms. The ____________ is the primary determinant of protein stability. ____________ and ____________ contribute relatively little to a protein’s stability.

A
native
denatured
hydrophobic effect
hydrogen bonding
ion pairing
29
Q

Studies of protein denaturation and renaturation indicate that the ____________ of a protein determines its three-dimensional structure.

A

primary structure

30
Q

Proteins fold to their native conformations via ____________ in which small elements of structure coalesce into larger structures.

A

direct pathways

31
Q

____________ facilitate protein folding in vivo by repeatedly binding and releasing a polypeptide in a(n) ____________ manner and providing it with a(n) ____________ in which to fold.

A

molecular chaperones
ATP-dependent
isolated environment

32
Q

Diseases caused by protein misfolding include the ____________, ____________, and the ____________.

A

amyloidoses
Alzheimer’s disease
transmissible spongiform encephalopathies (TSEs)