3.1-3.2 Flashcards

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1
Q

unique feature of each amino acid

A

R group

side chain

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2
Q

two common types of covalent bonds in proteins

A

peptide bonds

disulphide bonds b/w Cys

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3
Q

convention of writing proteins

A

amino terminal always written first

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4
Q

residue

A

individual aa when it is in a peptide

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5
Q

proteolysis

A

aka proteolytic cleavage
hydrolysis of a protein by another protein
specific means of cleaving peptide bonds

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6
Q

proteolytic enzyme

A

protease
protein that does the cutting
enzyme which cuts a protein

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7
Q

proteolytic cleavage

A

specific means of cleving peptide bonds

many enzymes cleave peptide bond adjacent to a specific aa

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8
Q

formation of peptide bond

A

lone pair on the amino group of 1 aa attacks the carboxyl group of the other aa
forming a N C C N C C pattern

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9
Q

trypsin cleavage

A

carboxyl side of Arg and Lys

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10
Q

chymotrypsin

A

cleaves adjacent to hydrophobic residues such as Phe

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11
Q

Cys special characteristics

A

has a reactive thiol ( SH) in its side chain
thiol aka sulfhydryl
reacts with thiol of another Cys to produce covalent S-S bond knwn as a disulphide bond

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12
Q

role of diS bond

A

important role in stabilizing tertiary protein structure

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13
Q

Cystine vs Cysteine

A

Cystine
refers to the molecule which is formed once the Cys residues are diS bonded to each other
Cysteine
refers to the individual aa

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14
Q

protein structure and function

A

each protein folds into a unique 3D structure that is required for protein to be functional

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15
Q

denatured

A

improperly folded proteins

are non functional

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16
Q

4 levels of protein folding

A
primary
secondary
tertiary
quaternary
all contributed to final 3D structure
each level depends on a certain type of bond
17
Q

primary sequence

A

simplest level of protein structure

order aa are bonded to each other in the polypep