Protein Folding: Search for Basic Physical Models

How a unique three-dimensional structure is rapidly formed from the linear sequence of a polypeptide is one of the important questions in contemporary science. Apart from biological context of in vivo protein folding (which has been studied only for a few proteins), the roles of the fundamental phys...

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Main Authors: Ivan Y. Torshin, Robert W. Harrison
Format: Article
Language:English
Published: Wiley 2003-01-01
Series:The Scientific World Journal
Online Access:http://dx.doi.org/10.1100/tsw.2003.50
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author Ivan Y. Torshin
Robert W. Harrison
author_facet Ivan Y. Torshin
Robert W. Harrison
author_sort Ivan Y. Torshin
collection DOAJ
description How a unique three-dimensional structure is rapidly formed from the linear sequence of a polypeptide is one of the important questions in contemporary science. Apart from biological context of in vivo protein folding (which has been studied only for a few proteins), the roles of the fundamental physical forces in the in vitro folding remain largely unstudied. Despite a degree of success in using descriptions based on statistical and/or thermodynamic approaches, few of the current models explicitly include more basic physical forces (such as electrostatics and Van Der Waals forces). Moreover, the present-day models rarely take into account that the protein folding is, essentially, a rapid process that produces a highly specific architecture. This review considers several physical models that may provide more direct links between sequence and tertiary structure in terms of the physical forces. In particular, elaboration of such simple models is likely to produce extremely effective computational techniques with value for modern genomics.
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spelling doaj-art-80ae983151ac4ed0bdca930b3efc674e2025-08-20T02:08:50ZengWileyThe Scientific World Journal1537-744X2003-01-01362363510.1100/tsw.2003.50Protein Folding: Search for Basic Physical ModelsIvan Y. Torshin0Robert W. Harrison1Department of Biology, Georgia State University, Atlanta, Georgia 30303, USADepartment of Biology, Georgia State University, Atlanta, Georgia 30303, USAHow a unique three-dimensional structure is rapidly formed from the linear sequence of a polypeptide is one of the important questions in contemporary science. Apart from biological context of in vivo protein folding (which has been studied only for a few proteins), the roles of the fundamental physical forces in the in vitro folding remain largely unstudied. Despite a degree of success in using descriptions based on statistical and/or thermodynamic approaches, few of the current models explicitly include more basic physical forces (such as electrostatics and Van Der Waals forces). Moreover, the present-day models rarely take into account that the protein folding is, essentially, a rapid process that produces a highly specific architecture. This review considers several physical models that may provide more direct links between sequence and tertiary structure in terms of the physical forces. In particular, elaboration of such simple models is likely to produce extremely effective computational techniques with value for modern genomics.http://dx.doi.org/10.1100/tsw.2003.50
spellingShingle Ivan Y. Torshin
Robert W. Harrison
Protein Folding: Search for Basic Physical Models
The Scientific World Journal
title Protein Folding: Search for Basic Physical Models
title_full Protein Folding: Search for Basic Physical Models
title_fullStr Protein Folding: Search for Basic Physical Models
title_full_unstemmed Protein Folding: Search for Basic Physical Models
title_short Protein Folding: Search for Basic Physical Models
title_sort protein folding search for basic physical models
url http://dx.doi.org/10.1100/tsw.2003.50
work_keys_str_mv AT ivanytorshin proteinfoldingsearchforbasicphysicalmodels
AT robertwharrison proteinfoldingsearchforbasicphysicalmodels