Literature DB >> 25225856

Frustration in biomolecules.

Diego U Ferreiro1, Elizabeth A Komives2, Peter G Wolynes3.   

Abstract

Biomolecules are the prime information processing elements of living matter. Most of these inanimate systems are polymers that compute their own structures and dynamics using as input seemingly random character strings of their sequence, following which they coalesce and perform integrated cellular functions. In large computational systems with finite interaction-codes, the appearance of conflicting goals is inevitable. Simple conflicting forces can lead to quite complex structures and behaviors, leading to the concept of frustration in condensed matter. We present here some basic ideas about frustration in biomolecules and how the frustration concept leads to a better appreciation of many aspects of the architecture of biomolecules, and especially how biomolecular structure connects to function by means of localized frustration. These ideas are simultaneously both seductively simple and perilously subtle to grasp completely. The energy landscape theory of protein folding provides a framework for quantifying frustration in large systems and has been implemented at many levels of description. We first review the notion of frustration from the areas of abstract logic and its uses in simple condensed matter systems. We discuss then how the frustration concept applies specifically to heteropolymers, testing folding landscape theory in computer simulations of protein models and in experimentally accessible systems. Studying the aspects of frustration averaged over many proteins provides ways to infer energy functions useful for reliable structure prediction. We discuss how frustration affects folding mechanisms. We review here how the biological functions of proteins are related to subtle local physical frustration effects and how frustration influences the appearance of metastable states, the nature of binding processes, catalysis and allosteric transitions. In this review, we also emphasize that frustration, far from being always a bad thing, is an essential feature of biomolecules that allows dynamics to be harnessed for function. In this way, we hope to illustrate how Frustration is a fundamental concept in molecular biology.

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Year:  2014        PMID: 25225856      PMCID: PMC4256721          DOI: 10.1017/S0033583514000092

Source DB:  PubMed          Journal:  Q Rev Biophys        ISSN: 0033-5835            Impact factor:   5.318


  209 in total

1.  A theoretical search for folding/unfolding nuclei in three-dimensional protein structures.

Authors:  O V Galzitskaya; A V Finkelstein
Journal:  Proc Natl Acad Sci U S A       Date:  1999-09-28       Impact factor: 11.205

Review 2.  Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance.

Authors:  H Jane Dyson; Peter E Wright
Journal:  Adv Protein Chem       Date:  2002

3.  Mutational analysis of kinetic partitioning in protein folding and protein-DNA binding.

Authors:  Ignacio E Sánchez; Diego U Ferreiro; Gonzalo de Prat Gay
Journal:  Protein Eng Des Sel       Date:  2010-09-27       Impact factor: 1.650

4.  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

5.  A unified model of protein dynamics.

Authors:  Hans Frauenfelder; Guo Chen; Joel Berendzen; Paul W Fenimore; Helén Jansson; Benjamin H McMahon; Izabela R Stroe; Jan Swenson; Robert D Young
Journal:  Proc Natl Acad Sci U S A       Date:  2009-02-27       Impact factor: 11.205

6.  Designing cooperativity into the designed protein Top7.

Authors:  Shilpa Yadahalli; Shachi Gosavi
Journal:  Proteins       Date:  2013-10-17

7.  Energy landscape of knotted protein folding.

Authors:  Joanna I Sułkowska; Jeffrey K Noel; Jose N Onuchic
Journal:  Proc Natl Acad Sci U S A       Date:  2012-08-13       Impact factor: 11.205

8.  Structure and properties of metallic glasses.

Authors:  P Chaudhari; D Turnbull
Journal:  Science       Date:  1978-01-06       Impact factor: 47.728

9.  Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models.

Authors:  Tural Aksel; Doug Barrick
Journal:  Methods Enzymol       Date:  2009       Impact factor: 1.600

10.  Protein frustratometer: a tool to localize energetic frustration in protein molecules.

Authors:  Michael Jenik; R Gonzalo Parra; Leandro G Radusky; Adrian Turjanski; Peter G Wolynes; Diego U Ferreiro
Journal:  Nucleic Acids Res       Date:  2012-05-29       Impact factor: 16.971

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  90 in total

1.  Molecular stripping in the NF-κB/IκB/DNA genetic regulatory network.

Authors:  Davit A Potoyan; Weihua Zheng; Elizabeth A Komives; Peter G Wolynes
Journal:  Proc Natl Acad Sci U S A       Date:  2015-12-23       Impact factor: 11.205

Review 2.  Protein folding transition path times from single molecule FRET.

Authors:  Hoi Sung Chung; William A Eaton
Journal:  Curr Opin Struct Biol       Date:  2017-11-05       Impact factor: 6.809

3.  Electrostatics, structure prediction, and the energy landscapes for protein folding and binding.

Authors:  Min-Yeh Tsai; Weihua Zheng; D Balamurugan; Nicholas P Schafer; Bobby L Kim; Margaret S Cheung; Peter G Wolynes
Journal:  Protein Sci       Date:  2015-08-08       Impact factor: 6.725

4.  Sliding Mechanism at a Coiled-Coil Interface.

Authors:  David Gomez; Yulian Gavrilov; Yaakov Levy
Journal:  Biophys J       Date:  2019-03-07       Impact factor: 4.033

5.  Knowledge-based entropies improve the identification of native protein structures.

Authors:  Kannan Sankar; Kejue Jia; Robert L Jernigan
Journal:  Proc Natl Acad Sci U S A       Date:  2017-03-06       Impact factor: 11.205

6.  The case for defined protein folding pathways.

Authors:  S Walter Englander; Leland Mayne
Journal:  Proc Natl Acad Sci U S A       Date:  2017-06-19       Impact factor: 11.205

7.  Physicochemical code for quinary protein interactions in Escherichia coli.

Authors:  Xin Mu; Seongil Choi; Lisa Lang; David Mowray; Nikolay V Dokholyan; Jens Danielsson; Mikael Oliveberg
Journal:  Proc Natl Acad Sci U S A       Date:  2017-05-23       Impact factor: 11.205

8.  Spontaneous refolding of the large multidomain protein malate synthase G proceeds through misfolding traps.

Authors:  Vipul Kumar; Tapan K Chaudhuri
Journal:  J Biol Chem       Date:  2018-06-29       Impact factor: 5.157

9.  On the Natural Structure of Amino Acid Patterns in Families of Protein Sequences.

Authors:  Pablo Turjanski; Diego U Ferreiro
Journal:  J Phys Chem B       Date:  2018-10-08       Impact factor: 2.991

10.  Contact Order Is a Determinant for the Dependence of GFP Folding on the Chaperonin GroEL.

Authors:  Boudhayan Bandyopadhyay; Tridib Mondal; Ron Unger; Amnon Horovitz
Journal:  Biophys J       Date:  2018-11-22       Impact factor: 4.033

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