BIOLCHEM 415 Study Guide - Midterm Guide: Zinc Finger, Nucleophile, Ultrasensitivity

• School: U of M
• Department: Biological Chemistry
• Course: BIOLCHEM 415
• Professor: Alex Ninfa

Document Summary

Cpk color coding (he will give the codes) Know the key principles, not all the fine details of examples. Do(cid:374)"t (cid:271)e ig(cid:374)o(cid:396)a(cid:374)t of ke(cid:455) discoveries of science. Format: all scantron, totally multiple choice, pictures, no short answer. Recognize the right answer; 40 questions in 50 minutes. Vitamins and enzymes they correlate with only know what was emphasized. So a low km (substrate concentration when reaction rate is half maximum) is better than high. Kcat = catalytic rate = k2 (the rate of the chemistry) Better the enzyme the lower the km (kcat/km) When k2 close to 0 then kd and km are about the same. Active substate: fraction of enzyme occupied is described by kd but when substrate is (cid:272)o(cid:374)(cid:448)e(cid:396)ted to p(cid:396)odu(cid:272)t the(cid:396)e is a(cid:374) e(cid:454)t(cid:396)a (cid:449)a(cid:455) that su(cid:271)st(cid:396)ate (cid:272)a(cid:374) (cid:272)o(cid:373)e out so that"s (cid:449)h(cid:455) k(cid:373) is always larger than kd. Competitive inhibition: e + s = es = p.