Lesson 3: Peptides & Classification of Proteins Flashcards

1
Q

What are peptides ?

A

Short sequences of amino acids linked together by covalent bonding

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2
Q

How are peptides formed ?

A

Carboxyl Group of an amino acid with an Amino Group of another amino acid

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3
Q

How is an aa read ?

A

From N-terminus

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4
Q

What is hydrolyctic cleavage ?

A

Cleaving peptide bonds to their constituant amino acids by the hydrolysis of peptide linkages

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5
Q

What is the Acid-Base behavior of a peptide dependent on ?

A

N-terminus , C-terminus , Ionizable R-group

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6
Q

What is labelling by FDNB ?

A

Amino terminal named as 1-fluro-2,4-dinitrobenzene

useful for the determination of primary structure of the peptide

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7
Q

What is labelling by FDNB ?

A

Amino terminal named as 1-fluro-2,4-dinitrobenzene

useful for the determination of primary structure of the peptide

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8
Q

How many aa residues does glutathione have ?

A

3

glutamate, cysteine and glycine

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9
Q

What are the functions of Glutathione ?

A

1)co-enzyme
2)participates in the second phase of the xenobiotic metabolism
3) reduce hydrogen peroxide (free radicle damaging to tissues) to water (antioxidant action)

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10
Q

How do trypsin and chymotrypsin bring about hydrolysis of peptide bonds ?

A

Through Proteolytic Cleavage

action is highly specific

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11
Q

What is Thyrotropin-releasing hormone (TRH) ?

A

a tripeptide released from the hypothalamus

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12
Q

How many aa residues does TRH have ?

A

3

Pyroglutamate-Histidine-Proline

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13
Q

What are enkephalins also known as ?

A

endogenous opiates

bind to receptors same to which synthetic opiates ex:morphine bind to

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14
Q

What does oxytocin do ? How many aa residues ?

A

Stimulates uterine contractions. 9

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15
Q

What does Glucagon do ? How many aa residues ?

A

Pancreatic hormone –> glucose homeostasis. 29

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16
Q

What is Partial Double Bond Character ?

A
  • single bond (C–N) does not show rotational freedom
  • the peptide bond is actually resonance hybrid of two electron isome
17
Q

aExplain φ and ψ Angles.

A
  1. Rotation around the nitrogen-and- α carbon bond is measured as the f φ(phi) angle
  2. Rotation around the peptide carbon and α -carbon bond as the c ψ(psi) angle

allow proteins to fold into secondary structures

18
Q

T/F: The peptide bond is positivaley charged.

A

False. Uncharged

19
Q

T/F: O and H are in CIS position

A

F. Trans

20
Q

What are the substituents of the peptide bond atoms ?

A

1) Alpha Carbon 1
2) Alpha Carbon 2
3) H atom
4) O atom

21
Q

What results in the H-Bond between the O and H in a peptide ?

A

The sharing of electrons between the C and the N.