Proteins Structure & Function Pt.2 Flashcards

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1
Q

Four types of secondary structures

A

*Alpha Helix
*Beta Sheet
Beta Turn
Omega Loop

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2
Q

Secondary structures are formed by

A

hydrogen bonds between N-H and C=O groups

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3
Q

Start the amino acid with the carbon with

A

a free amino group (N-term)

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4
Q

The end of the amino acid is

A

the free carbon with the carboxyl group (C-term)

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5
Q

Hydrogen bonds are formed between

A

H and electronegative atoms (Oxygen)

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6
Q

Alpha helix are stabilized by

A

intrachain hydrogen bonds

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7
Q

Beta strands form H bond two type of ways

A

Anti parallel and parallel

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8
Q

What determines if a protein is polar and non-polar

A

The R group

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9
Q

Folding is driven by the strong tendency of

A

hydrophobic (non-polar) amino acids to be excluded from water

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10
Q

Polar molecules are mostly found in the

A

cytoplasm

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11
Q

Unpaired N-H or C=O groups in peptides prefer

A

water (hydrophilic)

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12
Q

What interactions with the side chain stabilize the structure

A

Van der Waals interactions

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13
Q

Pairing the N-H or C=O groups with H bonds make them less

A

hydrophilic

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14
Q

The simplest quaternary structure is a dimer consisting of

A

two identical polypeptide chains called subunits

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15
Q

What determines if the polypeptide chain will form an alpha helix or a beta sheet

A

Amino acid residues

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16
Q

Denaturation

A

loss of structural integrity with accompanying loss of activity

17
Q

Proteins can be denatured by

A

*Temperature
*pH extremes
* Organic solvents
*Chaotropic agents

18
Q

The sequence alone determines

A

the native conformation