Proteins 2 Flashcards

1
Q

Refers to the arrangement / order of amino acids in a polypeptide

A

Primary structure

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2
Q

one-dimensional first step in specifying the 3 dimensional structure of proteins

A

Primary structure

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3
Q

it dictates the secondary, tertiary and quaternary structure of protein

A

Primary structure

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4
Q

Most stable structure

A

Primary structure

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5
Q
  • Determines the native and most frequently occurring secondary and tertiary
A

Primary structure

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6
Q

enables the whole chain to fold and curl in such a way to assume its final shape

A

Sequence (Primary structure)

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7
Q

consists of 40 or more amino acid residues

A

Oligopeptides

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8
Q

Conformations of amino acids in localized regions of a polypeptide chain

A

Secondary structure

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9
Q

local folding (exclusive of side chains)

A

Secondary structure

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10
Q

type of Structure with polar interaction

A

Secondary structure

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11
Q

Has INTERMOLECULAR HYDROGEN BONDS

A

??

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12
Q

In the peptide bond that link successive amino acid residues in a polypeptide chains, the electrons are somewhat

A

Delocalized

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13
Q
  • The polypeptide backbone has limited conformation flexibility
A

Secondary structure

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14
Q

2 Types of secondary structure

A

Alpha helix and beta pleated sheet

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15
Q

type of secondary structure in which a section of polypeptide chain coils into a spiral

A

Alpha helix structure

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16
Q

2 types of alpha helix (secondary) structure

A

Left and right handed spiral

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17
Q

Stabilizer of Secondary structure

A

Hydrogen bonds

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18
Q

How many amino acids are there per turn of alpha helix

A

3.6 amino acids

19
Q

distance of every turn / rise

A

5.4 angstroms along its axis

20
Q

Destabilizer of alpha helix

A

Proline, hydroxyproline and those that contain aromatic rings

21
Q

In alpha helix and beta pleated sheets, 8 atoms of each peptide bond lie in the same plane. True or False

A

False, 6 atoms

22
Q

In alpha helix, the N-H amino group and C=O carboxyl group point toward the same direction roughly ____ to the axis of the helix

23
Q

In alpha helix R-groups are

A

pointing OUTWARD from the helix

24
Q

A type of secondary structure in which two polypeptide chains or sections of the same polypeptide chain align parallel to each other

A

Beta pleated sheets

25
Types of Beta pleated sheets
Parallel and antiparallel
26
contains multiple polypeptide strands consist of line strands of polypeptide whose H-bonding requirements are met by bonding with neighboring strands creating parallel and antiparallel beta sheats
Beta pleated sheets
27
type of beta pleated sheets consists of neighboring chains that is ran in the same direction
Parallel
28
type of beta pleated sheet neighboring chains that ran in opposite direction in which each residues forms 2 HYDROGEN BONDS with neighboring strand
Antiparallel
29
In beta pleated sheets, the r-groups are
in alternating position, first above then below the plane of the sheet
30
Additional structure of secondary structure
Random coil
31
Collagen triple helix consists of
Glycine (1/3), Hydroxylysine and proline (proline can be a destabilizer)
32
Collagen triple helix follows what kind of force of attraction
Vander-wals
33
Collagen is what type of strcture
Secondary - alpha helix structure
34
type of structure that gives The complete three-dimensional arrangement of atoms of a polypeptide chain
Tertiary Structure
35
type of structure that uses nonpolar hydrophobic interaction and vander wals iforce of attraction
tertiary structure
36
type of structure that Gives the overall conformation of an entire polypeptide chain
Tertiary structure
37
Type of structure that gives the Spatial arrangement
tertiary structure
38
Tertiary structure is stabilized by
Hydrogen bond and 4 additional stability
39
type of structure that gives the 3D shape of a protein-- including the regular and irregular structures as well as the spatial arrangement of all its side chains
Tertiary structure
40
type of structure that is fully folded under physiological pH
Tertiary structure
41
Roles of transition metals (d-block series)
For stabilization of protein
42
Metals that form biologically important compounds
Transition metals
43
Coordination compoundsq
???
44
Tertiary structure stabilizer that forms disulfide bonds
Covalent bonds -- Cystine