Effects of fluidity on the ensemble structure of a membrane embedded α‐helical peptide-Reference-Cited by-同舟云学术

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Effects of fluidity on the ensemble structure of a membrane embedded α‐helical peptide

Published:2014-05-27 Issue:8 Volume:101 Page:895-902
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Eagleburger Michael K.¹,Cooley Jason W.¹,JiJi Renee D.¹

Affiliation:

1. Department of ChemistryUniversity of Missouri601 S College Ave, 125 Chemistry BuildingColumbia MO65211

Funder

National Science Foundation

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.22472

Reference56 articles.

1. How many drug targets are there?

2. Drugs and their molecular targets: an updated overview

3. The progress of membrane protein structure determination

4. Biophysical dissection of membrane proteins

5. Predicting transmembrane protein topology with a hidden markov model: application to complete genomes11Edited by F. Cohen

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2. A New Method to Determine the Transmembrane Conformation of Substrates in Intramembrane Proteolysis by Deep-UV Resonance Raman Spectroscopy;Methods in Enzymology;2017

3. Bilayer surface association of the pHLIP peptide promotes extensive backbone desolvation and helically-constrained structures;Biophysical Chemistry;2014-03

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