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C hem 375 S 2010 E xam 1 0 0.5 1 1.5 2 2.5 3 3.5 0 13 26 39 51 65 78 91 102 115 128 141 score Frequency Frequency Average = 112.4 = C+ Standard deviation = 16 A = 131+ B- = 113-117 A- = 126-130 C+ = 109-112 B+ = 122-125 C = 96-105 B= 118-121 C- = 85-95

Average = 112.4 = C+ Standard deviation = 16 A = 131+B- = 113-117 A- = 126-130 C+ = 109-112 B+ = 122-125 C = 96-105 B= 118-121 C- = 85-95

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Chem 375 S 2010 Exam 1

00.5

11.5

22.5

33.5

0

13

26

39

51

65

78

91

10

2

11

5

12

8

14

1

score

Fre

qu

en

cy

Frequency

Average = 112.4 = C+

Standard deviation = 16

A = 131+ B- = 113-117A- = 126-130 C+ = 109-112B+ = 122-125 C = 96-105B= 118-121 C- = 85-95

Table 11-1

Table 11-2

Figure 11-1

Page 325

Figure 11-2

Page 326

Figure 11-3

Figure 11-4

Page 327

Figure 11-5b

Figure 11-7

Figure 11-12 Biologically Important Nucleophiles and Electrophiles

Box 11-1

Figure 11-9 RNase S complexed with a nonhydrolyzable substrate.

Figure 11-10 Catalytic mechanism of RNase A.

Figure 11-10 part 1

Figure 11-10 part 2

Serine Proteases

We’re going to skip section 4 in Chapter 11 on lysozyme and continue with section 5:

Table 15-4 A Selection of Serine Proteases.

Pag

e 51

6

Figure 11-24

Figure 11-25 Trypsin

Figure 11-26

Figure 11-27

Figure 11-28

Figure 11-29

Figure 11-29 Catalytic mechanism ofthe serine proteases.

Pag

e 52

2

Catalytic mechanism of the serine proteases.

Pag

e 52

2

Catalytic mechanism of the serine proteases.

Pag

e 52

2

Catalytic mechanism of the serine proteases.

Pag

e 52

2

Pag

e 52

2

Catalytic mechanism of the serine proteases.

Pag

e 52

2

Pag

e 52

2

Figure 11-30a

Figure 11-30b

Figure 15-22 Relative positions of the active site residues in subtilisin, chymotrypsin, serine carboxypeptidase II, and ClpP protease.

Pag

e 52

1

Example of“divergent”evolution.

Example of“convergent”evolution.

Figure 11-31 Trypsin and Bovine Pancreatic Trypsin Inhibitor

Figure 11-33

Box 11-4a

Box 11-4b

Box 11-4c