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Folding scene investigation: membrane proteins

Investigations into protein folding have concentrated on experimentally tractable proteins with the result that membrane protein folding remains unsolved. New evidence is providing insight into the nature of the interactions stabilising the folded state of α-helical membrane proteins as well as givi...

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Detalles Bibliográficos
Autores principales: Booth, Paula J, Curnow, Paul
Formato: Texto
Lenguaje:English
Publicado: Elsevier Science 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2670978/
https://www.ncbi.nlm.nih.gov/pubmed/19157854
http://dx.doi.org/10.1016/j.sbi.2008.12.005
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author Booth, Paula J
Curnow, Paul
author_facet Booth, Paula J
Curnow, Paul
author_sort Booth, Paula J
collection PubMed
description Investigations into protein folding have concentrated on experimentally tractable proteins with the result that membrane protein folding remains unsolved. New evidence is providing insight into the nature of the interactions stabilising the folded state of α-helical membrane proteins as well as giving hints on the character of the folding transition state. These developments show that classical methods used for water-soluble proteins can be successfully adapted for membrane proteins. The advances, coupled with increasing numbers of solved crystal structures, augur well for future research into the mechanisms of membrane protein folding.
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spelling pubmed-26709782009-04-28 Folding scene investigation: membrane proteins Booth, Paula J Curnow, Paul Curr Opin Struct Biol Article Investigations into protein folding have concentrated on experimentally tractable proteins with the result that membrane protein folding remains unsolved. New evidence is providing insight into the nature of the interactions stabilising the folded state of α-helical membrane proteins as well as giving hints on the character of the folding transition state. These developments show that classical methods used for water-soluble proteins can be successfully adapted for membrane proteins. The advances, coupled with increasing numbers of solved crystal structures, augur well for future research into the mechanisms of membrane protein folding. Elsevier Science 2009-02 /pmc/articles/PMC2670978/ /pubmed/19157854 http://dx.doi.org/10.1016/j.sbi.2008.12.005 Text en © 2009 Elsevier Ltd. https://creativecommons.org/licenses/by/3.0/ Open Access under CC BY 3.0 (https://creativecommons.org/licenses/by/3.0/) license
spellingShingle Article
Booth, Paula J
Curnow, Paul
Folding scene investigation: membrane proteins
title Folding scene investigation: membrane proteins
title_full Folding scene investigation: membrane proteins
title_fullStr Folding scene investigation: membrane proteins
title_full_unstemmed Folding scene investigation: membrane proteins
title_short Folding scene investigation: membrane proteins
title_sort folding scene investigation: membrane proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2670978/
https://www.ncbi.nlm.nih.gov/pubmed/19157854
http://dx.doi.org/10.1016/j.sbi.2008.12.005
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