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
Q

what carries a postive charge at physiological pH

A

arg and lys

26
Q

what type of charge does histidine carry at physiological pH

A

can be positive or uncharged

27
Q

peptide bonds

A

linkages that connect amino acids to form polypeptide chains

28
Q

what are peptide bonds formed by

A

dehydration reaction

29
Q

what is the confirmation of a peptide bond

A

planar

30
Q

what is the primary structure of a protein

A

amino acid sequency

31
Q

what are the ends of a polypeptide chain

A

free amino group, free carbosylate group

32
Q

how are peptide sequences written

A

from N terminus to C terminus

33
Q

What are 2 ways we can view protein structures

A

X ray cystrallography and NMR spectroscopy

34
Q

what is the secondary protein structure

A

alpha helicies, and beta pleated sheets

35
Q

what is the structure of an alpha helix

A

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
Q

what hinders helix formation

A

proline
large buly side chains
multiple side chians of like charge

37
Q

what amino acids are often found in alpha helices

A

alanine, leucine, methionine