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Biochemistry

Quiz yourself by thinking what should be in each of the black spaces below before clicking on it to display the answer.
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Question
Answer
Alanine   A  
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Cysteine   C  
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aspartic acid   D  
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phenylalanine   F  
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glycine   G  
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histidine   H  
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isoleucine   I  
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Lysine   K  
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Leucine   L  
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Methionine   M  
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Asparagine   N  
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Proline   P  
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Glutamine   Q  
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Arginine   R  
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Serine   S  
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Threonine   T  
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Valine   V  
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Tryptophan   W  
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Tyrosine   Y  
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Glutamine   Z  
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Hydrophobic Amino Acids   glycine (G), alanine (A), proline (P), valine (V), leucine (L), isoleucine (I), phenylalanine (F), tyrosine (Y), tryptophan (W), methionine (M) GAPVLIFYWM  
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Branched chain Amino Acids   valine (V), leucine (L), isoleucine (I) VLI  
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non polar & hydrophobic amino acids   glycine (G), alanine (A), proline (P), valine (V), leucine (L), isoleucine (I), phenylalanine (F), methionine (M)  
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polar, uncharged amino acids   serine (S), threonine (T), tyrosine (Y), tryptophan (W), asparagine (N), glutamine (Q) STYWNQ  
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polar, uncharged OH groups and phosphorylate   serine (S), threonine (T), tyrosine (Y) STY  
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n-side chain   glycosylation  
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negatively charged amino acids   aspartate (D), glutamate (E) DE  
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backbone of Amino acids   alpha carbon + amino group + carbonyl group  
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positively charged basic molecules:   arginine (R), lysine (K), histidine (H) RKH  
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3 protein families   globular, fibrous, membrane spanning  
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in hemoglobin, iron can be   ferric (3+) or ferrous (2+)  
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heme binds oxygent   ferrous (2+)  
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primary hemoglobin in adults   HbA  
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fetal hemoglobin binds more readily to   carbon monoxide  
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if delta G is positive, amino acids remain   in hydrophobic side  
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if delta G is negative, amino acids migrate   into aqueous solution  
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What is the H+ concentration in a urine sample that has pH of 6   10^-6M  
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weak acids are   incompletely dissociated in solution  
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how many equivalents of base need to be added to an acid soution for the PH to equal the pKa   0.5  
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what is the best buffering range of the monoprotic acid MOPS, pka = 7.2   pH 6.5-8.5  
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due to the side group steric clash, almost all peptide bonds are   trans  
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which residues are most likely found in turns?   R, G, D  
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which residues are most likely to be found in DNA binding helixes?   K,R,Q  
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which residues are most likely to be found on the inside surface of a porin?   K,S,Q  
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Which amino acid is redox active?   C  
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which residues are most likely to be found on the inside surface of a protein?   M,L,F  
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changes in what level of structure are responsible for creating amyloid fibers?   secondary  
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what is a critical feature of the Michaelis-menten model of enzyme catalysis?   formation of an ES complex  
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at pH=8 mutation of histidine to which amino acid would be conservative?   N  
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In competitive inhibition, what does the inhibitor do?   it binds reversibly at the active site  
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in uncompetitive inhibition, what does the inhibitor do?   it binds only to the ES complex  
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in non competitive inhibition, what does the inhibitor do?   it lowers the characteristic V max of the enzyme  
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