Literature DB >> 2062107

Influence of point mutations on protein structure: probability of a neutral mutation.

E I Shakhnovich1, A M Gutin.   

Abstract

We investigate the probability X that a random mutation (i.e. the substitution in a random site of one amino acid residue by randomly chosen residue) will be a neutral one, i.e. it will not lead to a change in structure. Using a random energy model for the description of protein energy "levels" we show that this probability depends only on stiffness of a chain which is characterized by the number of conformations per peptide bond gamma. The result is X approximately gamma -8. The application of this result for protein engineering experiments and for possible scenario of neutral evolution is discussed.

Mesh:

Year:  1991        PMID: 2062107     DOI: 10.1016/s0022-5193(05)80097-9

Source DB:  PubMed          Journal:  J Theor Biol        ISSN: 0022-5193            Impact factor:   2.691


  7 in total

1.  Statistical significance of protein structure prediction by threading.

Authors:  L A Mirny; A V Finkelstein; E I Shakhnovich
Journal:  Proc Natl Acad Sci U S A       Date:  2000-08-29       Impact factor: 11.205

2.  Thermodynamic prediction of protein neutrality.

Authors:  Jesse D Bloom; Jonathan J Silberg; Claus O Wilke; D Allan Drummond; Christoph Adami; Frances H Arnold
Journal:  Proc Natl Acad Sci U S A       Date:  2005-01-11       Impact factor: 11.205

Review 3.  Protein folding thermodynamics and dynamics: where physics, chemistry, and biology meet.

Authors:  Eugene Shakhnovich
Journal:  Chem Rev       Date:  2006-05       Impact factor: 60.622

4.  Protein stability imposes limits on organism complexity and speed of molecular evolution.

Authors:  Konstantin B Zeldovich; Peiqiu Chen; Eugene I Shakhnovich
Journal:  Proc Natl Acad Sci U S A       Date:  2007-10-03       Impact factor: 11.205

5.  Conformation, energy, and folding ability of selected amino acid sequences.

Authors:  M Sasai
Journal:  Proc Natl Acad Sci U S A       Date:  1995-08-29       Impact factor: 11.205

6.  Monte Carlo simulations of beta-hairpin folding at constant temperature.

Authors:  S S Sung
Journal:  Biophys J       Date:  1999-01       Impact factor: 4.033

7.  Predict impact of single amino acid change upon protein structure.

Authors:  Christian Schaefer; Burkhard Rost
Journal:  BMC Genomics       Date:  2012-06-18       Impact factor: 3.969

  7 in total

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