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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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Formato: | Texto |
Lenguaje: | English |
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Elsevier Science
2009
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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. |
format | Text |
id | pubmed-2670978 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Elsevier Science |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT boothpaulaj foldingsceneinvestigationmembraneproteins AT curnowpaul foldingsceneinvestigationmembraneproteins |