Abstract
The elucidation of the three-dimensional structure of now over 100 proteins provides the basis for describing the nature of interactions stabilizing native protein structure. To understand the forces responsible for maintaining the native structure, it is necessary to analyze the contributions of the specific forces like a hydrogen bond, a salt bridge or a hydrophobic interaction to the overall stability of a protein. Using mutant proteins carrying a single amino acid substitution, specific interactions in a protein can be altered and the effect can be studied. In this paper the results of such studies on stability variants of human haemoglobin and of T4 phage lysozyme are described.
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We are grateful to A.N. Lane, J.A. Schellman, B.W. Matthews and J.N. Jansonius for critical reading of the manuscript and T. Balsiger for typing. The work on T4 phage lysozyme mutants was supported in part by grants from the NIH (GM 20066, GM 20195 and GM 21967) and from the M.J. Murdock Charitable Trust.
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Grütter, M.G., Hawkes, R.B. Mutations and the conformational stability of globular proteins. Naturwissenschaften 70, 434–438 (1983). https://doi.org/10.1007/BF01079609
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DOI: https://doi.org/10.1007/BF01079609