{[ promptMessage ]}

Bookmark it

{[ promptMessage ]}

2011 Biochem Review

2011 Biochem Review - BIOMG 3310 Course Review Tuesday...

Info iconThis preview shows pages 1–3. Sign up to view the full content.

View Full Document Right Arrow Icon
BIOMG 3310 Course Review Tuesday, December 6, 2011 PEPTIDES AND AMINO ACIDS general structure (do not memorize side chains) meaning of pK a and how to do Henderson-Hasselbalch calculation categories of AA (polar vs nonpolar) 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 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: largest single "driving force" is 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 R and T states cooperativity (O 2 ) allostery (O 2 , H + , BPG, CO) ENZYMES AND CATALYSIS
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full Document Right Arrow Icon
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: be able to draw an elementary rate constant corresponds to a particular G o barrier transition state: definition in general, what catalysts do to speed rxn 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 (but do not memorize equations for finding Km or Vm for inhib) 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) ENZYME REGULATION regulate enzyme concentration 1. synthesis and 2. 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 LIPIDS & BIOMEMBRANES lipid structure: fatty acids and triglycerides (Do know how to abbreviate; do not learn all the different phospholipid headgroups) lipid bilayer: general permeability properties membrane proteins: integral or peripheral membrane transport: passive transport vs
Background image of page 2
Image of page 3
This is the end of the preview. Sign up to access the rest of the document.

{[ snackBarMessage ]}

Page1 / 8

2011 Biochem Review - BIOMG 3310 Course Review Tuesday...

This preview shows document pages 1 - 3. Sign up to view the full document.

View Full Document Right Arrow Icon bookmark
Ask a homework question - tutors are online