NMR studies of differences in the conformations and dynamics of ligand complexes formed with mutant dihydrofolate reductases
Two mutants of Lactobacillus casei dihydrofolate reductase, Trp 21---Leu and Asp 26---Glu, have been prepared by using site-directed mutagenesis methods, and their ligand binding and structural properties have been compared with those of the wild-type enzyme. 1H, 13C, and 31P NMR studies have been c...
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Published in: | Biochemistry (Easton) Vol. 28; no. 3; pp. 1353 - 1362 |
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Main Authors: | , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
American Chemical Society
07-02-1989
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Subjects: | |
Online Access: | Get full text |
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