Conformational Flexibility of Enzyme Active Sites
Author:
Affiliation:
1. National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
Reference20 articles.
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2. EDWARDS, R.A., THERMAL-DENATURATION OF BETA-GALACTOSIDASE AND OF 2 SITE-SPECIFIC MUTANTS, BIOCHEMISTRY 29: 11001 (1990).
3. ENGELHARD, M, EQUILIBRIUM STUDIES ON REFOLDING AND REACTIVATION OF RABBIT-MUSCLE ALDOLASE AFTER ACID DISSOCIATION, EUROPEAN JOURNAL OF BIOCHEMISTRY 67: 447 (1976).
4. HO, Y.S., FORMATION OF A NEW FLUOROPHORE ON IRRADIATION OF CARBOXYMETHYLATED D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, NATURE 277: 245 (1979).
5. KOSHLAND, D.E., ROLE OF FLEXIBILITY IN SPECIFICITY, CONTROL AND EVOLUTION OF ENZYMES, FEBS LETTERS 62: E47 (1976).
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