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Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation

Structural fluctuation on microsecond to millisecond time scales has been reported to play an important role in proteins that undergo significant structural change during their expression of function. In these proteins, the structural change was obvious in the crystal structures. However, protein mo...

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Detalles Bibliográficos
Autores principales: Yanaka, Saeko, Ueno, Takamasa, Tsumoto, Kouhei, Sugase, Kenji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Biophysical Society of Japan (BSJ) 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4736795/
https://www.ncbi.nlm.nih.gov/pubmed/27493522
http://dx.doi.org/10.2142/biophysics.11.103
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author Yanaka, Saeko
Ueno, Takamasa
Tsumoto, Kouhei
Sugase, Kenji
author_facet Yanaka, Saeko
Ueno, Takamasa
Tsumoto, Kouhei
Sugase, Kenji
author_sort Yanaka, Saeko
collection PubMed
description Structural fluctuation on microsecond to millisecond time scales has been reported to play an important role in proteins that undergo significant structural change during their expression of function. In these proteins, the structural change was obvious in the crystal structures. However, protein motions in solution could contribute to the function of proteins, even if no significant structural difference is observed in crystal structure of different states while they function. In this review, we introduce our recent report on the stabilization mechanism of human leukocyte antigen, and the possibility of fluctuation contributing to several biophysical properties of proteins.
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spelling pubmed-47367952016-08-04 Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation Yanaka, Saeko Ueno, Takamasa Tsumoto, Kouhei Sugase, Kenji Biophysics (Nagoya-shi) Review Article Structural fluctuation on microsecond to millisecond time scales has been reported to play an important role in proteins that undergo significant structural change during their expression of function. In these proteins, the structural change was obvious in the crystal structures. However, protein motions in solution could contribute to the function of proteins, even if no significant structural difference is observed in crystal structure of different states while they function. In this review, we introduce our recent report on the stabilization mechanism of human leukocyte antigen, and the possibility of fluctuation contributing to several biophysical properties of proteins. The Biophysical Society of Japan (BSJ) 2015-04-18 /pmc/articles/PMC4736795/ /pubmed/27493522 http://dx.doi.org/10.2142/biophysics.11.103 Text en 2015 © The Biophysical Society of Japan This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Yanaka, Saeko
Ueno, Takamasa
Tsumoto, Kouhei
Sugase, Kenji
Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation
title Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation
title_full Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation
title_fullStr Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation
title_full_unstemmed Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation
title_short Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation
title_sort revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4736795/
https://www.ncbi.nlm.nih.gov/pubmed/27493522
http://dx.doi.org/10.2142/biophysics.11.103
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