English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Water permeation through gramicidin A: Desformylation and the double helix: A molecular dynamics study

de Groot, B. L., Tieleman, D. P., Pohl, P., & Grubmueller, H. (2002). Water permeation through gramicidin A: Desformylation and the double helix: A molecular dynamics study. Biophysical Journal, 82(6), 2934-2942. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B94RW-4TX1P02-B-1&_cdi=56421&_user=38661&_pii=S0006349502756348&_origin=search&_coverDate=06%2F30%2F2002&_sk=999179993&view=c&wchp=dGLbVtz-zSkzS&md5=80466bdea99a630e2f21b96e03c52b5e&ie=/sdarticle.pdf.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F3B0-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E5A1-3
Genre: Journal Article

Files

show Files
hide Files
:
17078.pdf (Publisher version), 0B
Name:
17078.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
de Groot, B. L.1, Author              
Tieleman, D. P., Author
Pohl, P., Author
Grubmueller, H.1, Author              
Affiliations:
1Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578630              

Content

show
hide
Free keywords: -
 Abstract: Multinanosecond molecular dynamics simulations of gramicidin A embedded in a dimyristoylphosphatidylcholine bilayer show a remarkable structural stability for both experimentally determined conformations: the head-to-head helical dimer and the double helix. Water permeability was found to be much higher in the double helical conformation, which is explained by lower hydrogen bond-mediated enthalpic barriers at the channel entrance and its larger pore size. Free-energy perturbation calculations show that the double helical structure is stabilized by the positive charges at the N termini introduced by the desformylation, whereas the helical dimer is destabilized. Together with the recent experimental observation that desformyl gramicidin conducts water hundredfold better than gramicidin, this suggests that desformyl gramicidin A predominantly occurs in the double helical conformation.

Details

show
hide
Language(s): eng - English
 Dates: 2002-06
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biophysical Journal
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 82 (6) Sequence Number: - Start / End Page: 2934 - 2942 Identifier: -