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ACTIVATION ENERGY BARRIER- |
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the height of potential energy between the reactants and products of a reaction |
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1/3 of all proteins, rigid & stable w/ H-bondingR-groups protrude out from center (2* structures) (NOTE: This is not in the list of keywords, but important to know) |
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extracellular deposits of pathologic insoluble fiber proteins, cause damage to area |
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disease characterized by amyloid deposits @ varible regions of immunoglobulin L-chains |
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hydrophobic side & hydrophilic side, terminals of strands in opposite ends |
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protein w/out its ligandbefore binding the ligand |
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1/3 of all proteins, form H-bonds with opposing strands, parallel or anti-parallel (2* structures) |
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fragments of L-chains (usually appear in urine w/ amyloidosis) |
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nonrepetitive, irregular 2* structure |
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refolding of proteins creates a template to denature normal prions, mass destruction |
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changes that disrupt ionic, hydrogen, & hydrophobic bonds to denature protein |
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muscle-brain CK unique to heart, measured to diagnose heart attack |
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position of AA side chains in 3D space, determines function of protein |
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portions of h- and L-chains of immunoglobins that do not vary |
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3-D space formed from continuous sequence of AA in polypeptide chain (3* structures) |
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critical for holding together & stabilizing tertiary into quaternary structures |
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insoluble proteins deposited by amyloidosis that cause damage where deposited |
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large pattern in of 3-D structures of many proteinsform fold families, perform function w/ other domains |
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2 (L) chains & 2 (H) chains joined by disulfide bonds, 12 domains, Y-shaped antibodies |
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glucose in blood binds to exposed amino group on protein (6-7% normal range) |
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heavy polypeptide chains (two) on immunoglobulins joined by disulfide bondsconstant domains |
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glucose attached to glycosylated hemoglobin on N-terminal of valineirreversibly bound to b-chains |
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oxygen binding tetramer protein, four oxygen binding sites, 2 alpha & 2 beta, sigmoidal curve |
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characteristics of protein that share same gene ancestry (same fold structure w/ different function) |
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- help 1* & 2* proteins form in the same family (HSP 70 helps proteins form out of ribosome) |
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4 pyrrole rings w/ nitrogen atoms binding to Fe2+ atom, tightly bound hydrophobic O2-binding pocket |
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proximal histidine binds to heme ring in myoglobin & hemeglobin |
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HYDROPHOBIC BINDING POCKET |
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- folded portion of helices of myoglobin & hemoglobin containing heme |
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Ka = [LP]/[L][P] k1/k2 association of ligand w/ binding site/dissociation of ligand-protein complex |
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Kd = 1/Ka dissociation constant for ligand-protein binding |
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light polypeptide chains(two) on antibodies joined @disulfide bond, variable domains for antigen binding |
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anything that binds to a protein |
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nonrepetitive, irregular 2* structure |
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one homogenous IgG produced by clone in bone marrow (spike on electrophoresis) |
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- arrangements of 2* structures related to each other (i.e. beta-alpha-loop-beta-alpha-loop) cannot exist alone |
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oxygen binding monomer protein, one oxygen binding site, all alpha helices, hyperbolic curve |
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NONENZYMATIC GLYCOSYLATION- |
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glucose in blood binds to exposed amino group on protein (irreversible) |
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extreme high or low can cause protein denaturation |
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hydrophobic residues on both sides, sheet twist in same direction, terminals the same |
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conformational changes to hemoglobin to allow O2 to bind in sigmoidal fashion |
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occur once the protein has already folded into 3D conformation |
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proteinaceous infectious agents protein that acts as a virus or bacteria, normally found in brain |
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normal conformation of protein prion |
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disease conformation of prion, enriched beta sheet structurescrapies in sheep (mad cow disease) |
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organic ligands that bind very tightlywill not dissociate (i.e. heme) |
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linear sequence of AAs in polypeptide chain |
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allows oxygen to bind to molecule, higher affinity to oxygen |
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combination of two or more 3* structures (-mers) homo- or hetero- (i.e. homodimer) |
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hold tertiary & quaternary structures together |
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short sequence of polypeptide chains forming structures (alpha helix & beta sheets) 3-30 |
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SERUM PROTEIN ELECTROPHORESIS- |
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test to indicate M-protein, sharp narrow spike confirms amyloid deposits |
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curve shape for hemoglobin on oxygen saturation graph |
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can cause proteins to denaturedisrupts the bonds holding proteins together |
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physically independent regions of 3* structures, can perform a physical or chemical task |
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will not allow binding to oxygeninhibited @ low pressures, low affinity to oxygen |
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folding patterns of 2* structures into 3-D conformations |
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- serum cardiac troponin Twill show increased in patients with congestive heart failure (CHF) |
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nonrepetitive, irregular 2* structure |
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portions of H- and L-chains of immunoglobins that vary to bind to specific antigens |
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