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non-polar aliphatic amino acid, side chain= methyl group |
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carbon in amino acids of proteins that contains amino & carboxyl groups as well as side chain |
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the COO- in amino acids that is bonded to the alpha carbon. |
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the amino group (C-NH3) in amino acids that is bonded to the the alpha carbon. |
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alternative versions of gene @ given locussame alleles=homozygous, different alleles=heterozygous |
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carboxyl group bonded to Nmost stable functional group |
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(ARG)-positive (basic) charged amino acid, side chain= four carbon w/ three amide groups(guanidinuim) |
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(ASN)- polar, uncharged amino acid, side chain= ethyl group w/ amide & carboxyl on end carbon |
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(ASP)- negative (acidic) charged amino acid, side chain= two carbon carboxylic acid group |
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(CK)- protein that exists as tissue specific isozyme (catalyze reactions) |
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CK-MB- isozyme of CK specific to cardiac musclecardiac muscle dies CK-MB is released into blood |
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CONSERVATIVE SUBSTITUTION |
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- replaces one amino acid with one of similar structure (i.e. ASP for GLU) |
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(CYS)- sulfur-containing amino acid, side chain= --C-SH |
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amino acid formed from oxidation of two cysteine molecules(disulfide bond)present in blood & tissues |
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inherited amino acid substitution in transport protein that reabsorbs cystine, arginine, & lysine |
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bond between to sulfhydryl groups of two CYShydrogens are removed during oxidation |
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proteins deriving from homologous genes but perform different functions (paralogs) |
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ELECTROSTATIC INTERACTIONS- |
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salt bonds that form between positive & negative charges of side chains |
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(GLU)- negative (acidic) charged amino acid, side chain= three carbon carboxylic acid group |
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(GLN)- polar, uncharged amino acid, side chain= propyl group w/ amide & carboxyl on end carbon |
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(GLY)- non-polar aliphatic amino acid, side chain= hydrogen (only amino acid w/o asymetric alpha carbon) |
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(HIS)- positive (basic) charged amino acid, side chain= ring structure w/ two amide groups |
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bulky, nonpolar, or aromatic side chains of amino acids not very soluble in water |
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polar, uncharged, and acid/base side chains of amino acids that can form hydrogen bonds w/ water |
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pH at which net charge on molecules is zero (neutral)helpful determining pH of AA @ given pH |
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(ILE)- nonpolar, aliphatic amino acid, side chain= 1-methyl propyl group |
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enzymes coming from the same primordial genome that differ in amino acid sequence but catalyze the same chemical reaction |
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all amino acids in mammalian proteins are L configuration |
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(LEU)- nonpolar, aliphatic amino acid, side chain= 2-methyl propyl group |
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(LYS)- positively (basic) charged amino acid, side chain= four carbon w/ primary amino on terminal carbon |
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- bioengineered insulin where the position of PRO @ B28 and LYS @ B29 is switched |
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(MET)- sulfur-containing amino acid, side chain= --C-C-S-C |
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charge of AA at a given pH5 carry net chargesalpha group charge + R-group charge |
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a loss of hydrogen or oxygen in a molecule; disulfide bond & cystine are more oxidized |
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bond between carboxyl group of one AA and amino group of next AAalso an amide bond |
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(isoelectric point) pH at which net charge zero; pI = (pKa alpha-amino + pKa alpha-carboxyl)/2 |
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(PHE)- non-polar aromatic amino acid, side chain= phenyl group |
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variants of alleles that appear with significant frequency in population (i.e. sickle cell allele) |
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substitution of one base for another in DNA sequence of nucleotides |
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(PRO)- nonpolar, aliphatic amino acid, side chain= triangle propyl group attached to amine |
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when two or more amino acids combine to form a peptide bond, the element of water is removed, and what remains of each amino acid is called an amino acid residue. Residues lack either the hydrogen atoms of the amino group, an oxygen from the carboxyl group, or both. |
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the additional chemical side chain of each different amino acid; determines the function of the amino acid |
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a gain of hydrogen or oxygen in a molecule; sulfhydryl group & cysteine are more reduced |
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- bonds between positive & negative side chains5 AA can form salt bonds (ASP,GLU,HIS,LYS,ARG) |
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(SER)- polar, uncharged amino acid, side chain= methanol group |
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caused by point mutation in DNA that changes hemoglobin; change is from glutamate to valine |
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two cysteine residues that combine to form a disulfide bondcystine |
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(THR)- polar, uncharged amino acid, side chain= 1-methyl methanol group |
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(TRP)- polar, aromatic amino acid, side chain= two ring structural group |
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(TYR)- polar, aromatic amino acid, side chain= phenyl alcohol group |
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(VAL)- nonpolar, aliphatic amino acid, side chain= iso-propyl group |
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TAGS (Thr, Asn, Gln, Ser) |
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