peptides 9/14 Flashcards

1
Q

what are alpha amino acids joined by and what is the reaction between

A

joined by an amide linkage and a condensation rxn bt an amino and carboxylic acid; the bond can be broken by a hydrolysis rxn

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2
Q

what are the amide linkages of a peptide called

A

peptide bonds

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3
Q

what is the difference between naming for amino acids with a few residues vs many

A

few: oligopeptide
many: polypeptide

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4
Q

what do all peptides have

A

amino terminal and carboxyl terminal

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5
Q

what do names or primary structures start with

A

N-terminal (amine group)

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6
Q

how are peptide structures described

A

baackbone and side chains

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7
Q

since amino acids may be post translationally modified…

A

peptides and proteins may consist of more than 20 diff amino acids

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8
Q

since peptides have characteristic ionization behavior and pI

A

ion exchange chromatography and isoelectric focusing can be used to isolate them

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9
Q

where are disulfide bonds found

A

extracellularly

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10
Q

how can molecular weight be estimated

A

110/residue

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11
Q

oligomeric proteins have

A

two or more identical subunits called protomers such as hemoglobin that has 2 alpha/beta protomers

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12
Q

what is composition and how is it determined

A

proportion that each amino acid contributes to the total; determined by complete acid hydrolysis followed by HPLC (high performance liquid chromatography)

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13
Q

what are prosthetic groups

A

contribute to protein function

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14
Q

what are conjugated proteins

A

proteins with prosthetic groups

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15
Q

what are halo enzymes/proteins and apoenzymes/proteins

A

halo=protein with prosthetic group attached

apo=protein without prosthetic group attached

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16
Q

what is primary structure

A

amino acid sequence (covalent structure includes crosslinks like disulfide bonds)

17
Q

secondary structure

A

3D conformations that are stable because of characteristics and backbone

18
Q

tertiary structure

A

3D folding of the peptide

19
Q

quaternary structure

A

association of subunits in multisubunit proteins

20
Q

denaturation

A

loss of native, functional secondary, tertiary, and quarternary structure

21
Q

what is the ultimate goal of protein structure studies

A
  1. understand functional contribution of each amino acid
  2. understand functional difference between alleles and variants
  3. be able to manipulate protein function by drugs and/or gene therapy