Literature DB >> 8622938

Why are some proteins structures so common?

S Govindarajan1, R A Goldstein.   

Abstract

Many biological proteins are observed to fold into one of a limited number of structural motifs. By considering the requirements imposed on proteins by their need to fold rapidly, and the ease with which such requirements can be fulfilled as a function of the native structure, we can explain why certain structures are repeatedly observed among proteins with negligible sequence similarity. This work has implications for the understanding of protein sequence structure relationships as well as protein evolution.

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Year:  1996        PMID： 8622938      PMCID： PMC39609          DOI： 10.1073/pnas.93.8.3341

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  27 in total

1.  Inverse protein folding problem: designing polymer sequences.

Authors:  K Yue; K A Dill
Journal:  Proc Natl Acad Sci U S A       Date:  1992-05-01       Impact factor: 11.205

2.  The energy landscapes and motions of proteins.

Authors:  H Frauenfelder; S G Sligar; P G Wolynes
Journal:  Science       Date:  1991-12-13       Impact factor: 47.728

3.  Phosphorescence reveals a continued slow annealing of the protein core following reactivation of Escherichia coli alkaline phosphatase.

Authors:  V Subramaniam; N C Bergenhem; A Gafni; D G Steel
Journal:  Biochemistry       Date:  1995-01-31       Impact factor: 3.162

4.  Impact of local and non-local interactions on thermodynamics and kinetics of protein folding.

Authors:  V I Abkevich; A M Gutin; E I Shakhnovich
Journal:  J Mol Biol       Date:  1995-09-29       Impact factor: 5.469

5.  LINUS: a hierarchic procedure to predict the fold of a protein.

Authors:  R Srinivasan; G D Rose
Journal:  Proteins       Date:  1995-06

6.  Toward an outline of the topography of a realistic protein-folding funnel.

Authors:  J N Onuchic; P G Wolynes; Z Luthey-Schulten; N D Socci
Journal:  Proc Natl Acad Sci U S A       Date:  1995-04-11       Impact factor: 11.205

7.  How does a protein fold?

Authors:  A Sali; E Shakhnovich; M Karplus
Journal:  Nature       Date:  1994-05-19       Impact factor: 49.962

8.  Kinematics and thermodynamics of a folding heteropolymer.

Authors:  M Fukugita; D Lancaster; M G Mitchard
Journal:  Proc Natl Acad Sci U S A       Date:  1993-07-01       Impact factor: 11.205

9.  Kinetics of protein folding. A lattice model study of the requirements for folding to the native state.

Authors:  A Sali; E Shakhnovich; M Karplus
Journal:  J Mol Biol       Date:  1994-02-04       Impact factor: 5.469

10.  Spin glasses and the statistical mechanics of protein folding.

Authors:  J D Bryngelson; P G Wolynes
Journal:  Proc Natl Acad Sci U S A       Date:  1987-11       Impact factor: 11.205
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  34 in total

1.  Evolution of functionality in lattice proteins.

Authors:  P D Williams; D D Pollock; R A Goldstein
Journal:  J Mol Graph Model       Date:  2001       Impact factor: 2.518

2.  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

3.  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

4.  Intra-chain 3D segment swapping spawns the evolution of new multidomain protein architectures.

Authors:  András Szilágyi; Yang Zhang; Péter Závodszky
Journal:  J Mol Biol       Date:  2011-11-04       Impact factor: 5.469

5.  Natural selection of more designable folds: a mechanism for thermophilic adaptation.

Authors:  Jeremy L England; Boris E Shakhnovich; Eugene I Shakhnovich
Journal:  Proc Natl Acad Sci U S A       Date:  2003-07-03       Impact factor: 11.205

6.  Strategies for selection from protein libraries composed of de novo designed secondary structure modules.

Authors:  Tomoaki Matsuura; Andreas Plückthun
Journal:  Orig Life Evol Biosph       Date:  2004-02       Impact factor: 1.950

7.  Imprint of evolution on protein structures.

Authors:  Guido Tiana; Boris E Shakhnovich; Nikolay V Dokholyan; Eugene I Shakhnovich
Journal:  Proc Natl Acad Sci U S A       Date:  2004-02-17       Impact factor: 11.205

8.  Protein structure and evolutionary history determine sequence space topology.

Authors:  Boris E Shakhnovich; Eric Deeds; Charles Delisi; Eugene Shakhnovich
Journal:  Genome Res       Date:  2005-03       Impact factor: 9.043

9.  Comparing folding codes in simple heteropolymer models of protein evolutionary landscape: robustness of the superfunnel paradigm.

Authors:  Richard Wroe; Erich Bornberg-Bauer; Hue Sun Chan
Journal:  Biophys J       Date:  2004-10-22       Impact factor: 4.033

10.  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
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