Course Review - BIOBM331 Course Review Monday, December 3,...

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BIOBM331 Course Review Monday, December 3, 2007 PEPTIDES AND AMINO ACIDS general structure (do not memorize side chains) meaning of pK a categories of AA draw peptide bond PROTEIN STRUCTURE forces folding constraints: bond angles, lengths, and size of atoms Φ , Ψ rotation restrictions Ramachandran Map draw Ramachandran Map or describe in words OBSERVED STRUCTURES α -helix, β -sheet, turns, collagen: general properties (don't memorize Φ , Ψ ) I, II, III, IV and structural domains transient IV structure (e.g. transcription complexes; insulin signaling complex) commonly observed structures: Zn-fingers; P-loops FORMATION/LOSS OF PROTEIN STRUCTURE G o vs structural coordinates know how to show relatively lower or higher stability on such diagrams denaturation: loss of function caused by partial/complete loss of native struct. folding: driven by hydrophobic interaction info to fold is in sequence "molten globule" some proteins assist folding or prevent aggregation: disulfide isomerase prolyl isomerase chaperones-- how they work HEMOGLOBIN special properties: sat. with O 2 in lungs, but gives up O 2 to tissue low O 2 affinity when BPG bound low O 2 affinity at low pH higher O 2 affinity for fetal Hb role of ion pairs in deoxyHb
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R and T states cooperativity (O 2 ) allostery (O 2 , H + , BPG, CO) ENZYMES AND CATALYSIS specificity: what is the basis? what are cofactors? rxn rate increase: basic kinetics; data of kinetics; why rxns take time G o vs progress of rxn an elementary rate constant corresponds to a particula r G o barrier transition state: definition what catalysts do: enzyme kinetics: Michaelis-Menten kinetics: know/use equation K m , V m (know definitions) V m = k cat [E] total , but k cat can be combo of rate constants Lineweaver-Burk plot enzyme inhibition: charge on ionizable AA residues (pH effects) competitive, non-competitive, irreversible chymotrypsin (do not memorize each intermediate) (no mech. question on final exam) ENZYME REGULATION regulate enzyme concentration synthesis and degradation regulate enzyme activity allosteric (R and T states): non-covalent or covalent aspartate carbamoyl transferase glycogen phosphorylase phosphofructokinase pyruvate kinase covalent zymogens phosphorylation/dephosphorylation lipid structure: fatty acids and triglycerides (know how to abbreviate; do not learn all the different
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This note was uploaded on 02/19/2008 for the course BIOBM 3310 taught by Professor Feigenson,gw during the Fall '07 term at Cornell University (Engineering School).

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Course Review - BIOBM331 Course Review Monday, December 3,...

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