Crystal Versus Solution Structures of Enzymes: NMR Spectroscopy of a Crystalline Serine Protease
Author:
Affiliation:
1. Francis Bitter National Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, MA02139.
2. Department of Biochemistry, Tufts University, School of Medicine, Boston, MA 02111.
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
Reference21 articles.
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2. BACHOVCHIN, W.W., N-15 NUCLEAR MAGNETIC-RESONANCE SPECTROSCOPY - STATE OF HISTIDINE IN CATALYTIC TRIAD OF ALPHA-LYTIC PROTEASE - IMPLICATIONS FOR CHARGE-RELAY MECHANISM OF PEPTIDE-BOND CLEAVAGE BY SERINE PROTEASES, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 100: 8041 (1978).
3. BLOW, D.M., ROLE OF A BURIED ACID GROUP IN MECHANISM OF ACTION OF CHYMOTRYPSIN, NATURE 221: 337 (1969).
4. BODE, W, REFINED CRYSTAL-STRUCTURE OF BOVINE BETA-TRYPSIN AT 1.8 A RESOLUTION .2. CRYSTALLOGRAPHIC REFINEMENT, CALCIUM-BINDING SITE, BENZAMIDINE BINDING-SITE AND ACTIVE-SITE AT PH 7.0, JOURNAL OF MOLECULAR BIOLOGY 98: 693 (1975).
5. BRAYER, G.D., MOLECULAR-STRUCTURE OF THE ALPHA-LYTIC PROTEASE FROM MYXOBACTER-495 AT 2-8-A RESOLUTION, JOURNAL OF MOLECULAR BIOLOGY 131: 743 (1979).
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