Response of a Protein Structure to Cavity-Creating Mutations and Its Relation to the Hydrophobic Effect
Author:
Affiliation:
1. Institute of Molecular Biology, Howard Hughes Medical Institute, and Department of Physics, University of Oregon, Eugene, OR 97403.
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
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3. ALBER, T, REPLACEMENTS OF PRO86 IN PHAGE-T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY, SCIENCE 239: 631 (1988).
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5. BRANDTS, J.F., THERMODYNAMICS OF PROTEIN DENATURATION .3. DENATURATION OF RIBONUCLEASE IN WATER AND IN AQUEOUS UREA AND AQUEOUS ETHANOL MIXTURES, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 89: 4826 (1967).
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