Literature DB >> 10753815

Ab initio protein folding.

D J Osguthorpe1.   

Abstract

Ab initio protein folding methods have been developing rapidly over the past few years and, at the last Critical assessment of methods of protein structure prediction (CASP) meeting, it was shown that important progress has been made in generating structure from sequence. Both methods based on statistical potentials and methods using physics-based potentials have shown improvements. Most current methods use statistics-based potentials and the development of these is ongoing. Additionally, the inclusion of multiple sequence data in the algorithms in order to aid in finding the native structure is a common theme. The use of physics-based potentials is less developed, which means that less progress has been made in understanding why a sequence forms a structure.

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Year:  2000        PMID: 10753815     DOI: 10.1016/s0959-440x(00)00067-1

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  4 in total

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Journal:  Ann Appl Stat       Date:  2010-06-01       Impact factor: 2.083

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Journal:  Chem Rev       Date:  2022-05-16       Impact factor: 72.087

3.  In silico and in vivo studies of molecular structures and mechanisms of AtPCS1 protein involved in binding arsenite and/or cadmium in plant cells.

Authors:  Noor Nahar; Aminur Rahman; Maria Moś; Tomasz Warzecha; Sibdas Ghosh; Khaled Hossain; Neelu N Nawani; Abul Mandal
Journal:  J Mol Model       Date:  2014-02-20       Impact factor: 1.810

4.  Local Protein Structure Refinement via Molecular Dynamics Simulations with locPREFMD.

Authors:  Michael Feig
Journal:  J Chem Inf Model       Date:  2016-07-13       Impact factor: 4.956

  4 in total

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