Isotope-edited IR spectroscopy for the study of membrane proteins

Fourier transform infrared (FTIR) spectroscopy has long been a powerful tool for structural analysis of membrane proteins. However, because of difficulties in resolving contributions from individual residues, most of the derived measurements tend to yield average properties for the system under stud...

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Detalles Bibliográficos
Autor principal: Arkin, Isaiah T
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Ltd. 2006
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7185810/
https://www.ncbi.nlm.nih.gov/pubmed/16935550
http://dx.doi.org/10.1016/j.cbpa.2006.08.013
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author Arkin, Isaiah T
author_facet Arkin, Isaiah T
author_sort Arkin, Isaiah T
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description Fourier transform infrared (FTIR) spectroscopy has long been a powerful tool for structural analysis of membrane proteins. However, because of difficulties in resolving contributions from individual residues, most of the derived measurements tend to yield average properties for the system under study. Isotope editing, through its ability to resolve individual vibrations, establishes FTIR as a method that is capable of yielding accurate structural data on individual sites in a protein.
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spelling pubmed-71858102020-04-28 Isotope-edited IR spectroscopy for the study of membrane proteins Arkin, Isaiah T Curr Opin Chem Biol Article Fourier transform infrared (FTIR) spectroscopy has long been a powerful tool for structural analysis of membrane proteins. However, because of difficulties in resolving contributions from individual residues, most of the derived measurements tend to yield average properties for the system under study. Isotope editing, through its ability to resolve individual vibrations, establishes FTIR as a method that is capable of yielding accurate structural data on individual sites in a protein. Elsevier Ltd. 2006-10 2006-08-28 /pmc/articles/PMC7185810/ /pubmed/16935550 http://dx.doi.org/10.1016/j.cbpa.2006.08.013 Text en Copyright © 2006 Elsevier Ltd. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Arkin, Isaiah T
Isotope-edited IR spectroscopy for the study of membrane proteins
title Isotope-edited IR spectroscopy for the study of membrane proteins
title_full Isotope-edited IR spectroscopy for the study of membrane proteins
title_fullStr Isotope-edited IR spectroscopy for the study of membrane proteins
title_full_unstemmed Isotope-edited IR spectroscopy for the study of membrane proteins
title_short Isotope-edited IR spectroscopy for the study of membrane proteins
title_sort isotope-edited ir spectroscopy for the study of membrane proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7185810/
https://www.ncbi.nlm.nih.gov/pubmed/16935550
http://dx.doi.org/10.1016/j.cbpa.2006.08.013
work_keys_str_mv AT arkinisaiaht isotopeeditedirspectroscopyforthestudyofmembraneproteins

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