Figure 6'01 XRay structure of chymotrypsin'

1
Figure 6.01 X-Ray structure of chymotrypsin.
2
Figure 6.02 Reaction coordinate diagram for the
reaction AB C
A BC
3
Figure 6.03 Reaction coordinate diagram for a
reaction in which reactants and products have
different free energies.
4
Figure 6.04 Effect of a catalyst on a chemical
reaction.
5
Figure 6.05 Amino acid side chains that can act
as acid-base catalysts.
6
Figure 6.06 Reaction coordinate diagram for a
reaction accelerated by covalent catalysis.
7
Figure 6.07 Protein groups that can act as
covalent catalysts.
8
Figure 6.08 The catalytic triad of chymotrypsin.
9
Figure 6.09 The catalytic mechanism of
chymotrypsin and other serine proteases.
10
Figure 6.11 Effect of very tight substrate
binding on enzyme catalysis.
11
Figure 6.12 Transition state stabilization in the
osyanion hole.
12
Figure 6.13 Formation of a low-barrier hydrogen
bond during catalysis in chymotrypsin.
13
Figure 6.14 Proximity and orientation effect in
catalysis.
14
Figure 6.18 Specificity pockets of three serine
proteases.
15
Figure 6.19 Activation of chymotrypsinogen.