Application of Solution NMR to Structural Studies on α-Helical Integral Membrane Proteins
A large portion of proteins in living organisms are membrane proteins which play critical roles in the biology of the cell, from maintenance of the biological membrane integrity to communication of cells with their surroundings. To understand their mechanism of action, structural information is esse...
Main Authors: | , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2017-08-01
|
Series: | Molecules |
Subjects: | |
Online Access: | https://www.mdpi.com/1420-3049/22/8/1347 |
id |
doaj-da4fdb3cf43f45409b3e5d6201c2de56 |
---|---|
record_format |
Article |
spelling |
doaj-da4fdb3cf43f45409b3e5d6201c2de562020-11-25T00:47:13ZengMDPI AGMolecules1420-30492017-08-01228134710.3390/molecules22081347molecules22081347Application of Solution NMR to Structural Studies on α-Helical Integral Membrane ProteinsDae-Won Sim0Zhenwei Lu1Hyung-Sik Won2Seu-Na Lee3Min-Duk Seo4Bong-Jin Lee5Ji-Hun Kim6Department of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungbuk 27478, KoreaDepartment of Biochemistry, Vanderbilt University, Nashville, TN 37204, USADepartment of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungbuk 27478, KoreaDepartment of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungbuk 27478, KoreaDepartment of Molecular Science and Technology & College of Pharmacy, Ajou University, Suwon 16499, KoreaThe Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Gwanak-gu, Seoul 151-742, KoreaCollege of Pharmacy, Chungbuk National University, Cheongju 28160, Chungbuk, KoreaA large portion of proteins in living organisms are membrane proteins which play critical roles in the biology of the cell, from maintenance of the biological membrane integrity to communication of cells with their surroundings. To understand their mechanism of action, structural information is essential. Nevertheless, structure determination of transmembrane proteins is still a challenging area, even though recently the number of deposited structures of membrane proteins in the PDB has rapidly increased thanks to the efforts using X-ray crystallography, electron microscopy, and solid and solution nuclear magnetic resonance (NMR) technology. Among these technologies, solution NMR is a powerful tool for studying protein-protein, protein-ligand interactions and protein dynamics at a wide range of time scales as well as structure determination of membrane proteins. This review provides general and useful guideline for membrane protein sample preparation and the choice of membrane-mimetic media, which are the key step for successful structural analysis. Furthermore, this review provides an opportunity to look at recent applications of solution NMR to structural studies on α-helical membrane proteins through some success stories.https://www.mdpi.com/1420-3049/22/8/1347solution NMRα-helical integral membrane proteinstructuremembrane-mimeticsisotope labeling |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Dae-Won Sim Zhenwei Lu Hyung-Sik Won Seu-Na Lee Min-Duk Seo Bong-Jin Lee Ji-Hun Kim |
spellingShingle |
Dae-Won Sim Zhenwei Lu Hyung-Sik Won Seu-Na Lee Min-Duk Seo Bong-Jin Lee Ji-Hun Kim Application of Solution NMR to Structural Studies on α-Helical Integral Membrane Proteins Molecules solution NMR α-helical integral membrane protein structure membrane-mimetics isotope labeling |
author_facet |
Dae-Won Sim Zhenwei Lu Hyung-Sik Won Seu-Na Lee Min-Duk Seo Bong-Jin Lee Ji-Hun Kim |
author_sort |
Dae-Won Sim |
title |
Application of Solution NMR to Structural Studies on α-Helical Integral Membrane Proteins |
title_short |
Application of Solution NMR to Structural Studies on α-Helical Integral Membrane Proteins |
title_full |
Application of Solution NMR to Structural Studies on α-Helical Integral Membrane Proteins |
title_fullStr |
Application of Solution NMR to Structural Studies on α-Helical Integral Membrane Proteins |
title_full_unstemmed |
Application of Solution NMR to Structural Studies on α-Helical Integral Membrane Proteins |
title_sort |
application of solution nmr to structural studies on α-helical integral membrane proteins |
publisher |
MDPI AG |
series |
Molecules |
issn |
1420-3049 |
publishDate |
2017-08-01 |
description |
A large portion of proteins in living organisms are membrane proteins which play critical roles in the biology of the cell, from maintenance of the biological membrane integrity to communication of cells with their surroundings. To understand their mechanism of action, structural information is essential. Nevertheless, structure determination of transmembrane proteins is still a challenging area, even though recently the number of deposited structures of membrane proteins in the PDB has rapidly increased thanks to the efforts using X-ray crystallography, electron microscopy, and solid and solution nuclear magnetic resonance (NMR) technology. Among these technologies, solution NMR is a powerful tool for studying protein-protein, protein-ligand interactions and protein dynamics at a wide range of time scales as well as structure determination of membrane proteins. This review provides general and useful guideline for membrane protein sample preparation and the choice of membrane-mimetic media, which are the key step for successful structural analysis. Furthermore, this review provides an opportunity to look at recent applications of solution NMR to structural studies on α-helical membrane proteins through some success stories. |
topic |
solution NMR α-helical integral membrane protein structure membrane-mimetics isotope labeling |
url |
https://www.mdpi.com/1420-3049/22/8/1347 |
work_keys_str_mv |
AT daewonsim applicationofsolutionnmrtostructuralstudiesonahelicalintegralmembraneproteins AT zhenweilu applicationofsolutionnmrtostructuralstudiesonahelicalintegralmembraneproteins AT hyungsikwon applicationofsolutionnmrtostructuralstudiesonahelicalintegralmembraneproteins AT seunalee applicationofsolutionnmrtostructuralstudiesonahelicalintegralmembraneproteins AT mindukseo applicationofsolutionnmrtostructuralstudiesonahelicalintegralmembraneproteins AT bongjinlee applicationofsolutionnmrtostructuralstudiesonahelicalintegralmembraneproteins AT jihunkim applicationofsolutionnmrtostructuralstudiesonahelicalintegralmembraneproteins |
_version_ |
1725261255652933632 |