2010 COURSE REVIEW - BIOMG 3310 COURSE REVIEW THIS...

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BIOMG 3310 COURSE REVIEW PEPTIDES AND AMINO ACIDS general structure (do not memorize side chains) meaning of pK a and how to use Henderson-Hasselbalch Eq draw peptide bond PROTEIN STRUCTURE forces folding constraints: bond angles, lengths, and size of atoms Φ, Ψ rotation restrictions Ramachandran Map understand what info is in a Ramachandran Map! OBSERVED STRUCTURES α -helix, β -sheet, turns, collagen: general properties (don't memorize Φ, Ψ ) I, II, III, IV and folds ("structural domains"): be able to define transient IV structure (e.g. transcription complexes; insulin signaling complex) commonly observed structures: Zn-fingers; P-loops THIS "KNOW/DON'T KNOW" INFO APPLIES TO BOTH REGULAR AND MAKE-UP EXAMS
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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. protein 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: Be able to describe in words, or show on a graph 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 R and T states cooperativity (O 2 )
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ENZYMES AND CATALYSIS 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 detailed mechanism question on final exam) specificity: what is the basis? what are cofactors?
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2010 COURSE REVIEW - BIOMG 3310 COURSE REVIEW THIS...

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