Tertiary structure Flashcards

1
Q

what are tertiary structures ultimately determined by?

A

amino acid sequence
environment in which protein is found

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2
Q

what kind of environment do soluble proteins require

A

aqueous environments

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3
Q

where do membrane protein structures fold properly, and how can this environment be imitated?

A

membrane
detergents

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4
Q

which forces are critical in determining tertiary structure

A

noncovalent
hydrophobic
van der waals
H-bonds
ionic interactions

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5
Q

what is the native conformation

A

low-energy functional state

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6
Q

what is the delta G for folding into native conformation

A

-100 kJ/mol

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7
Q

T or F: there is only one stable functional state of native conformation

A

False

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8
Q

how are functional states of native conformation created?

A

ligands, flexible portions of proteins, breathing

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9
Q

which technique can yield general characteristics of secondary structure

A

circular dichroism

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10
Q

which technique can yield detailed atomic information

A

x-ray crystallography, protein NMR

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11
Q

how does circular dichroism work?

A

differential absorption of left and right circularly polarized light

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12
Q

what type of structure is most sensitive to circular dichroism

A

secondary

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13
Q

what can be seen through CD spectra

A

alpha helices, beta sheets, random coils and irregular structures

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14
Q

what kind of experiments is CD particularly useful for

A

denaturation/ renaturation

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15
Q

how does xray crystallography work

A

protein preparations (pure) require pure samples which are then exposed to X-rays

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16
Q

what information does X-ray crystallography provide

A

electron density used to build models

17
Q

higher or lower resolution will provide better X-ray diffraction

A

lower

18
Q

which regions on Xray crystallography will reveal the location of nuclei

A

electron density

19
Q

what are the pros of X-ray crystallography

A

highly detailed resolutions
rapid solutions
useful for large proteins/complexes

20
Q

what are the cons of X-ray crystallography

A

crystal growth
diffract
static
no hydrogens

21
Q

what information does NMR provide

A

3D, distance restraints

22
Q

what can protein NMR be combined with

A

geometry information

23
Q

what does the range of solutions in protein NMR reflecrt?

A

motion and error

24
Q

what are the pros of protein NMR

A

dynamic information
proteins are in solution