Structure of proteins I Flashcards

1
Q

functions of proteins

A

catalyst for reactions
regulate gene transciption
mediatory of immune response
components of CT

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2
Q

what are the structure and function of a protein determined by

A

amino acid sequence of its polypeptide chain

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3
Q

feature of alpha-amino acid

A

central alpha-carbon

alpha carbon is asymmetric (except glycine)

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4
Q

what type of amino acids are found in mamalian proteins

A

L-amino acids

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5
Q

what amino acid is a secondary amine

A

proline

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6
Q

what groups is an alpha carbon covalently bound to

A

alpha amine
alpha carboxylic acid
hydrogen
R group

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7
Q

what gives each amino acid its unique chemical and physical properties

A

the R group

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8
Q

zwitterion

A

molecule having both positive and negative charges

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9
Q

what are the non polar aliphatic amino acids

A

glycine, alanine, valine, leucine, isoleucine, methionine, proline

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10
Q

where are the non-polar aliphatic amino acids typically found

A

in interior of globular proteins

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11
Q

what is unique about methionine

A

contains sulfur

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12
Q

what are the aromatic amino acids

A

phenyalanine
tyrosine
tryptophan

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13
Q

what type of property do aromtic amino acids ahve

A

hydrophobic

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14
Q

why does tyrosine ahve soem polarity

A

because of the OH group

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15
Q

why is tryptophan slightly polar

A

ring nitrogen

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16
Q

what are the pola runcharged amino acids

A
serine
threonine
cysterin
asparagine
glutamine
17
Q

where are the polar, uncharged amino acids found

A

interior and exterior of proteins

18
Q

what do polar, uncharged amino acids readily form

A

hydrogen bonds

19
Q

what is unqiue about cysteine

A

contains sulfur, readily forms disulfie bridges

20
Q

the hydroxyl groups of serine and threonine serve as what

A

phosphate acceptors in protein kinase reactions

21
Q

what are the amino acids with ionizable side chains

A

aspartate gluatmate

22
Q

what are asp adn glu considered to be

A

acidic amino acids

23
Q

what are the basic amino acids

A

lysine, arginine, histidine

24
Q

what carries a negative charge at physiological pH

A

asp adn glu

25
what carries a postive charge at physiological pH
arg and lys
26
what type of charge does histidine carry at physiological pH
can be positive or uncharged
27
peptide bonds
linkages that connect amino acids to form polypeptide chains
28
what are peptide bonds formed by
dehydration reaction
29
what is the confirmation of a peptide bond
planar
30
what is the primary structure of a protein
amino acid sequency
31
what are the ends of a polypeptide chain
free amino group, free carbosylate group
32
how are peptide sequences written
from N terminus to C terminus
33
What are 2 ways we can view protein structures
X ray cystrallography and NMR spectroscopy
34
what is the secondary protein structure
alpha helicies, and beta pleated sheets
35
what is the structure of an alpha helix
clockwise spiral each C=O is hydrogen bonding to H-N group 4 amino acid residues down each turn contains 3.5 amino acid residues
36
what hinders helix formation
proline large buly side chains multiple side chians of like charge
37
what amino acids are often found in alpha helices
alanine, leucine, methionine