Literature DB >> 8592696

Why do protein architectures have Boltzmann-like statistics?

A V Finkelstein1, A M Gutin.   

Abstract

A theoretical study has shown that the occurrence of various structural elements in stable folds of random copolymers is exponentially dependent on the own energy of the element. A similar occurrence-on-energy dependence is observed in globular proteins from the level of amino acid conformations to the level of overall architectures. Thus, the structural features stabilized by many random sequences are typical of globular proteins while the features rarely observed in proteins are those which are stabilized by only a minor part of the random sequences.

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Year:  1995        PMID: 8592696     DOI: 10.1002/prot.340230204

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  43 in total

1.  Analysis of knowledge-based protein-ligand potentials using a self-consistent method.

Authors:  J Shimada; A V Ishchenko; E I Shakhnovich
Journal:  Protein Sci       Date:  2000-04       Impact factor: 6.725

2.  Composites of local structure propensities: evidence for local encoding of long-range structure.

Authors:  David Shortle
Journal:  Protein Sci       Date:  2002-01       Impact factor: 6.725

3.  Construction and characterization of protein libraries composed of secondary structure modules.

Authors:  Tomoaki Matsuura; Andreas Ernst; Andreas Plückthun
Journal:  Protein Sci       Date:  2002-11       Impact factor: 6.725

4.  Expanding protein universe and its origin from the biological Big Bang.

Authors:  Nikolay V Dokholyan; Boris Shakhnovich; Eugene I Shakhnovich
Journal:  Proc Natl Acad Sci U S A       Date:  2002-10-16       Impact factor: 11.205

5.  Boltzmann-type distribution of side-chain conformation in proteins.

Authors:  Glenn L Butterfoss; Jan Hermans
Journal:  Protein Sci       Date:  2003-12       Impact factor: 6.725

6.  Propensities, probabilities, and the Boltzmann hypothesis.

Authors:  David Shortle
Journal:  Protein Sci       Date:  2003-06       Impact factor: 6.725

7.  Pair potentials for protein folding: choice of reference states and sensitivity of predicted native states to variations in the interaction schemes.

Authors:  M R Betancourt; D Thirumalai
Journal:  Protein Sci       Date:  1999-02       Impact factor: 6.725

8.  Sequence specificity, statistical potentials, and three-dimensional structure prediction with self-correcting distance geometry calculations of beta-sheet formation in proteins.

Authors:  H Zhu; W Braun
Journal:  Protein Sci       Date:  1999-02       Impact factor: 6.725

9.  Physical-chemical determinants of coil conformations in globular proteins.

Authors:  Lauren L Perskie; George D Rose
Journal:  Protein Sci       Date:  2010-06       Impact factor: 6.725

Review 10.  Protein folding thermodynamics and dynamics: where physics, chemistry, and biology meet.

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

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