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AA & Protein Struct.
WVSOM Class of 2012 Amino Acids and Protein Structure
| Question | Answer |
|---|---|
| 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
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