BIOCHEM 1 - protein structure and organization Flashcards

1
Q

Defined by the amino acid sequence

A

primary structure

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2
Q

structure composed of Rigid planar peptide groups

A

primary structure

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3
Q

Rotation about the α-carbon

αC – Carbonyl Carbon

A

Ψ (psi):

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4
Q

Rotation about the α-carbon

αC – N

A

Ф (phi):

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5
Q

structure with Regular Folding

A

secondary structure

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6
Q

interaction in secondary structure

A

Interaction: H-bond between the amide proton and carbonyl oxygen

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7
Q

Spatial arrangement of the atoms in the polypeptide chain

A

secondary structure

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8
Q

The PRIMARY structure dictates the ____ structure.

A

Secondary

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9
Q

type of secondary structure having

Intramolecular H-bond

A

alpha helix

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10
Q

pitch of alpha helix

A

Pitch: 5.4 Å

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11
Q

aa residue per turn of alpha helix

A

3.6

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12
Q

Kinds of α – helix

A

right handed

left handed

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13
Q

where are the R-groups located in alpha helix

A

outside the helix

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14
Q

type of secondary structure

Intrachain or interchain H-bond

A

beta pleated sheet

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15
Q

Two types of beta sheet

A

Parallel pleated sheet

Antiparallel pleated sheet

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16
Q

Other secondary structures

A

Other helix structures
Random coils
Reverse turns or β bends

17
Q

Combinations of α and β-strands

A

supersecondary structures

18
Q

examples of supersecondary structures

A

Ex: βαβ unit, αα unit, β-meander and Greek key

19
Q

– repetitive supersecondary structures

A

Motif

20
Q

type of protein structure

Three-dimensonal arrangement

A

tertiary structure

21
Q

Important aspect of tertiary structure

A

arrangement of the side chains of aa residues

22
Q

Types of protein conformation

A

Globular proteins

Fibrous proteins

23
Q

type of protein structure

Spatial arrangement of polypeptide subunits

A

quaternary structure

24
Q

Interactions of quaternary structure:

A

same with tertiary structure

25
Q

Loss of high level of structural organization of protein

A

denaturation

26
Q

It is the sequence of amino acids linked by peptide bonds.

▪ The backbone of a peptide chain or protein.

A

primary structure

27
Q

the location of prosthetic groups is shown in this structure

A

tertiary

28
Q

structures which repeat over and over in a secondary structure

A

supersecondary structure

29
Q

disulfide bonds are most important in this type of structure

A

tertiary structure

30
Q

a supersecondary region, often shared by protein, having a specific function

A

domain

31
Q

vitamin necessary for hydroxyproline synthesis

A

C

32
Q

AA important in holding 3 strands of collagen together

A

hydroxyproline

33
Q

fibrous proteins can be composed of either helical or Beta sheet structures, true or false

A

TRUE

34
Q

Independently folded regions of proteins

A

domains