1C69
| |
1C6B
| |
1C63
| |
1C68
| |
1C6C
| |
1C6D
| |
1C6E
| |
1C6F
| |
1C6P
| |
1C61
| |
1C6G
| |
1C6Q
| |
1C60
| |
1C62
| |
1C6H
| |
1C6J
| |
1C6I
| |
1C6T
| |
1C6M
| |
1C6K
| |
1C6L
| |
1C66
| |
1C6N
| |
1C6A
| |
1CV1
| T4 LYSOZYME MUTANT V111M | Descriptor: | 2-HYDROXYETHYL DISULFIDE, CHLORIDE ION, LYSOZYME | Authors: | Gassner, N.C, Baase, W.A, Lindstrom, J.D, Lu, J, Matthews, B.W. | Deposit date: | 1999-08-20 | Release date: | 1999-11-10 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry, 38, 1999
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