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Biochemistry Lecture > Proteins 2 > Flashcards

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

A

Parallel

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
Q

Types of Beta pleated sheets

A

Parallel and antiparallel

26
Q

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

A

Beta pleated sheets

27
Q

type of beta pleated sheets consists of neighboring chains that is ran in the same direction

A

Parallel

28
Q

type of beta pleated sheet neighboring chains that ran in opposite direction in which each residues forms 2 HYDROGEN BONDS with neighboring strand

A

Antiparallel

29
Q

In beta pleated sheets, the r-groups are

A

in alternating position, first above then below the plane of the sheet

30
Q

Additional structure of secondary structure

A

Random coil

31
Q

Collagen triple helix consists of

A

Glycine (1/3), Hydroxylysine and proline (proline can be a destabilizer)

32
Q

Collagen triple helix follows what kind of force of attraction

A

Vander-wals

33
Q

Collagen is what type of strcture

A

Secondary - alpha helix structure

34
Q

type of structure that gives The complete three-dimensional arrangement of atoms of a polypeptide chain

A

Tertiary Structure

35
Q

type of structure that uses nonpolar hydrophobic interaction and vander wals iforce of attraction

A

tertiary structure

36
Q

type of structure that Gives the overall conformation of an entire polypeptide chain

A

Tertiary structure

37
Q

Type of structure that gives the Spatial arrangement

A

tertiary structure

38
Q

Tertiary structure is stabilized by

A

Hydrogen bond and 4 additional stability

39
Q

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

A

Tertiary structure

40
Q

type of structure that is fully folded under physiological pH

A

Tertiary structure

41
Q

Roles of transition metals (d-block series)

A

For stabilization of protein

42
Q

Metals that form biologically important compounds

A

Transition metals

43
Q

Coordination compoundsq

A

???

44
Q

Tertiary structure stabilizer that forms disulfide bonds

A

Covalent bonds – Cystine

Biochemistry Lecture (8 decks)

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