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. 1985 Mar;82(6):1697–1700. doi: 10.1073/pnas.82.6.1697

Structure of proteins with single-site mutations: a minimum perturbation approach.

H H Shih, J Brady, M Karplus
PMCID: PMC397339  PMID: 3856851

Abstract

A large number of mutant proteins with single amino acid substitutions are now being produced. The ability to predict the structural changes expected from such mutations would aid greatly in the efficient utilization of the mutagenic techniques and in the interpretation of the changes in stability and function that result. A minimum perturbation approach is suggested as a first step in such structural predictions and is tested by application to a recently isolated variant of the hemagglutinin glycoprotein. The agreement between the predicted structure and that inferred from the x-ray refinement is encouraging and provides support for the proposed modeling procedure.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Gelin B. R., Karplus M. Side-chain torsional potentials: effect of dipeptide, protein, and solvent environment. Biochemistry. 1979 Apr 3;18(7):1256–1268. doi: 10.1021/bi00574a022. [DOI] [PubMed] [Google Scholar]
  2. Greer J. Model of a specific interaction. Salt-bridges form between prothrombin and its activating enzyme blood clotting factor Xa. J Mol Biol. 1981 Dec 25;153(4):1043–1053. doi: 10.1016/0022-2836(81)90466-6. [DOI] [PubMed] [Google Scholar]
  3. Grütter M. G., Hawkes R. B., Matthews B. W. Molecular basis of thermostability in the lysozyme from bacteriophage T4. Nature. 1979 Feb 22;277(5698):667–669. doi: 10.1038/277667a0. [DOI] [PubMed] [Google Scholar]
  4. Hawkes R., Grutter M. G., Schellman J. Thermodynamic stability and point mutations of bacteriophage T4 lysozyme. J Mol Biol. 1984 May 15;175(2):195–212. doi: 10.1016/0022-2836(84)90474-1. [DOI] [PubMed] [Google Scholar]
  5. Hecht M. H., Nelson H. C., Sauer R. T. Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding. Proc Natl Acad Sci U S A. 1983 May;80(9):2676–2680. doi: 10.1073/pnas.80.9.2676. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Janin J., Wodak S. Conformation of amino acid side-chains in proteins. J Mol Biol. 1978 Nov 5;125(3):357–386. doi: 10.1016/0022-2836(78)90408-4. [DOI] [PubMed] [Google Scholar]
  7. Knossow M., Daniels R. S., Douglas A. R., Skehel J. J., Wiley D. C. Three-dimensional structure of an antigenic mutant of the influenza virus haemagglutinin. Nature. 1984 Oct 18;311(5987):678–680. doi: 10.1038/311678a0. [DOI] [PubMed] [Google Scholar]
  8. Novotný J., Bruccoleri R., Karplus M. An analysis of incorrectly folded protein models. Implications for structure predictions. J Mol Biol. 1984 Aug 25;177(4):787–818. doi: 10.1016/0022-2836(84)90049-4. [DOI] [PubMed] [Google Scholar]
  9. Némethy G., Scheraga H. A. Protein folding. Q Rev Biophys. 1977 Aug;10(3):239–252. doi: 10.1017/s0033583500002936. [DOI] [PubMed] [Google Scholar]
  10. Ulmer K. M. Protein engineering. Science. 1983 Feb 11;219(4585):666–671. doi: 10.1126/science.6572017. [DOI] [PubMed] [Google Scholar]
  11. Weiss M. A., Karplus M., Patel D. J., Sauer R. T. Solution NMR studies of intact lambda repressor. J Biomol Struct Dyn. 1983 Oct;1(1):151–157. doi: 10.1080/07391102.1983.10507431. [DOI] [PubMed] [Google Scholar]
  12. Wiley D. C., Wilson I. A., Skehel J. J. Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature. 1981 Jan 29;289(5796):373–378. doi: 10.1038/289373a0. [DOI] [PubMed] [Google Scholar]

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