MCB 124 Lecture Notes - Lecture 1: Van Der Waals Force, Excluded Volume, Equilibrium Constant
21 Apr 2017
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Structure determines function by specificity which is created by a folded/ binded surfaces. If you have 2 states i and j , they both have different energies. We can determine the proportions of molecules in each state. ( assume all states are occupied, even if little). When air molecules hit you, they transfer kinetic energy. Rule of thumb: at 25c, every 1. 4kcal/mol of deltag corresponds to 10-fold change in keq. (about 1-2 h-bonds per decade) Interatomic interactions: chemical bonds (cause atoms to stick together)- in protein structures are essentially stable and non-deformable. Clatherate is formed around it: highly ordered structures are entropically unfavorable. R,k,h(charged basic), a,v,i,l,f,c,m,p,y,w (hydrophobic: w-absorbance at 280nm, y-at 280, f-at 250. To know how much free e(cid:374)e(cid:396)g(cid:455) ho(cid:449) (cid:373)u(cid:272)h does t(cid:396)(cid:455)ptopha(cid:374) (cid:272)o(cid:374)t(cid:396)i(cid:271)ute to the o(cid:448)e(cid:396)all foldi(cid:374)g of a p(cid:396)otei(cid:374). Taking protein out of order would change the interactions- so (cid:272)a(cid:374)"t do that.
