Next Article in Journal
Fenton Discoloration of Ultrasonicated Purple Cactus Pear Juice
Next Article in Special Issue
A Unique and Simple Approach to Improve Sensitivity in 15N-NMR Relaxation Measurements for NH3+ Groups: Application to a Protein-DNA Complex
Previous Article in Journal
Inositol Derivatives and Phenolic Compounds from the Roots of Taraxacum coreanum
Previous Article in Special Issue
Capillary-Inserted Rotor Design for HRµMAS NMR-Based Metabolomics on Mass-Limited Neurospheres
Article Menu
Issue 8 (August) cover image

Export Article

Open AccessReview
Molecules 2017, 22(8), 1347; doi:10.3390/molecules22081347

Application of Solution NMR to Structural Studies on α-Helical Integral Membrane Proteins

1
Department of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungbuk 27478, Korea
2
Department of Biochemistry, Vanderbilt University, Nashville, TN 37204, USA
3
Department of Molecular Science and Technology & College of Pharmacy, Ajou University, Suwon 16499, Korea
4
The Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Gwanak-gu, Seoul 151-742, Korea
5
College of Pharmacy, Chungbuk National University, Cheongju 28160, Chungbuk, Korea
These authors contributed equally to this paper.
*
Authors to whom correspondence should be addressed.
Received: 31 July 2017 / Revised: 10 August 2017 / Accepted: 12 August 2017 / Published: 15 August 2017
(This article belongs to the Special Issue Recent Advances in Biomolecular NMR Spectroscopy)
View Full-Text   |   Download PDF [4547 KB, uploaded 15 August 2017]   |  

Abstract

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. View Full-Text
Keywords: solution NMR; α-helical integral membrane protein; structure; membrane-mimetics; isotope labeling solution NMR; α-helical integral membrane protein; structure; membrane-mimetics; isotope labeling
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Sim, D.-W.; Lu, Z.; Won, H.-S.; Lee, S.-N.; Seo, M.-D.; Lee, B.-J.; Kim, J.-H. Application of Solution NMR to Structural Studies on α-Helical Integral Membrane Proteins. Molecules 2017, 22, 1347.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top