Peptides Flashcards

1
Q

A compound containing
two amino acids is specifically called a

A

dipeptide

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1
Q

is an unbranched
chain of amino acids, each joined to the next by a peptide bond

A

peptide

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2
Q

three amino acids joined together in
a chain constitute a

A

tripeptide

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3
Q

s loosely used to refer
to peptides with 10 to 20 amino acid residues

A

oligopeptide

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4
Q

is a long unbranched chain of amino acids, each
joined to the next by a peptide bond.

A

Polypeptide

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5
Q

is a covalent bond between the carboxyl group of one amino acid and the amino group of another amino acid.

A

Peptide bond

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6
Q

The end with the free H3N+ group is called

A

N terminal end

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6
Q

end with the free COO- group is called the

A

C terminal end

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7
Q

s the portion of an amino acid structure that remains, after the release of H2O, when an amino acid participates in peptide bond formation as it becomes part of a peptide chain

A

amino acid residue

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8
Q

The two best-known peptide hormones, both produced by the pituitary gland,

A

oxytocin
and vasopressin

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9
Q

are pentapeptide neurotransmitters produced by the brain itself that bind at
receptor sites in the brain to reduce pain

A

Enkephalins

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10
Q

Met-enkephalin

A

Tyr–Gly–Gly–Phe–Met

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11
Q

Leu-enkephalin

A

Tyr–Gly–Gly–Phe–Leu

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12
Q

is a protein in which
only one peptide chain is present

A

monomeric protein

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13
Q

is a protein in which more than one
peptide chain is present

A

multimeric protein

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14
Q

is a protein in which only amino acid residues are present

A

simple protein

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15
Q

The peptide chains present in multimeric proteins are called

A

protein subunits.

16
Q

is a protein that has one or more non amino acid entities present in its structure in addition to one or more peptide chains.

A

conjugated protein

18
Q

is a non-amino acid group present in a conjugated protein.

A

prosthetic group

19
Q

contain carbohydrate groups

A

glycoproteins

20
Q

contain lipid prosthetic groups

A

Lipoproteins

21
Q

contain a specific metal, and so on.

A

metalloproteins

22
Q

These four protein structural levels, listed in order of increasing complexity, are?

A

Primary, secondary, tertiary, quaternary structure

23
Who work the to determined the primary structure?
Frederick Sanger
24
is the order in which amino acids are linked together in a protein
Primary protein
25
is the arrangement in space adopted by the backbone portion of a protein.
Secondary protein structure
26
Give me The two most common types of secondary structure are..
Alpha Helix and Beta pleated sheet
27
s a protein secondary structure in which a single protein chain adopts a shape that resembles a coiled spring (helix), with the coil configuration maintained by hydrogen bonds
alpha helix structure
28
is a protein secondary structure in which two fully extended protein chain segments in the same or different molecules are held together by hydrogen bonds
beta pleated sheet structure
29
is the overall three-dimensional shape of a protein that results from the interactions between amino acid side chains (R groups) that are widely separated from each other within a peptide chain
Tertiary protein structure
30
Give me the Four types of attractive interactions contribute to the tertiary structure of a protein
Covalent Disulfide bonds, Electrostatic attractions, hydrogen bonds, hydrophobic attractions.
31
is the organization among the various peptide chains in a multimeric protein
Quaternary protein structure
32
is a protein whose molecules have an elongated shape with one dimension much longer than the others
fibrous protein
33
is a protein whose molecules have peptide chains that are folded into spherical or globular shapes
A globular protein
34
is a protein that is found associated with a membrane system of a cell
membrane protein
35
this hemoglobin has a greater affinity for oxygen than the mother’s hemoglobin
fetal hemoglobin
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