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AA & Protein Struct.

WVSOM Class of 2012 Amino Acids and Protein Structure

at normal ph, amino groups have what charge? positive
what are the hydrophobic amino acids? glycine (G), alanine (A), proline (P), valine (V), leucine (L), isoleucine (I), phenylalanine (F), tyrosine (Y), tryptophan (W), methionine (M): (GAPVLIFYWM)
what are the branched chain amino acids? valine (V), leucine (L), isoleucine (I)
which amino acids are non-polar and hydrophobic? glycine (G), alanine (A), proline (P), valine (V), leucine (L), isoleucine (I), phenylalanine (F), methionine (M): (GAPVLIFM)
which amino acids are polar uncharged? serine (S), threonine (T), tyrosine (Y), tryptophan (W), asparagine (N), glutamine (Q): (STYWNQ)
out of the polar uncharged amino acids, which have OH groups and can phosphorylate? serine (S), threonine (T), tyrosine (Y): (STY)
the n-side chain is a common site for what? glycosylation
what are the negatively charged amino acids? aspartate (D), and glutamate (E): (D&E)
what is the backbone of an amino acid? an alpha carbon + an amino group + a carboxyl group
aspartate and glutamate can form what bonds? ionic and hydrogen bonds
what are the positively charged basic molecules? arginine (R), lysine (K), and histidine (H)
how are arginine and lysine frequently modified? acetylation and methylation
the pka of a histidine side chain is what? what does this help it to make? 6.0; a good buffer
cystine is held by what kind of bonds? disulfide
excess cystine can form what in humans? calculi
phenylalanine is what structure? what does this cause it to do? aromatic, it can stack
what amino acid causes kinks in the peptide chain? proline
what are the 3 protein families? globular, fibrous, and membrane-spanning
keratin is a classic example of what kind of bonds? disulfide
rhodopsin has non-polar chains on the ____ and polar chains on the ____ surface, interior
in hemoglobin, iron can be what forms? Ferric (3+) or Ferrous (2+)
which heme can bind oxygen? ferrous (2+)
heme group is a pocket of hydrophobic amino acids and what? histidine residues
myoglobin is small and can therefore do what? leak out of damaged cells
what is the primary hemoglobin in adults? HbA
if the body wants to release oxygen, which form of hemoglobin will it use? if it wants to uptake oxygen? taut, relaxed
when histidine is protonated, what happens to the oxygen in hemoglobin? it gets released
2,3-BPG forms when? during glycolysis
what form of hemoglobin does 2,3-BPG stabilize? taut form
methemoglobin binds to which Fe form? what must next happen 3+, it must be reduced back ot 2+
decreased NADH methemoglobin reductase results in what condition? methemoglobinemia (blue people of kentucky)
fetal hemoglobin binds more readily with what gas? carbon monoxide
what letter represents leucine? l
what letter represents phenylalanine? f
what letter represents tyrosine? y
what letter represents tryptopham? w
what letter represents asparagine? n
what letter represents glutamine? q
what letter represents threonine? t
what letter represents aspartate? d
what letter represents glutamate? e
what letter represents lysine? k
Created by: mhassan