English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics.

Chevelkov, V., Xue, Y., Linser, R., Skrynnikov, N. R., & Reif, B. (2010). Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics. Journal of the American Chemical Society, 132(14), 5015-5017. doi:10.1021/ja100645k.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0018-EA89-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-3B7D-0
Genre: Journal Article

Files

show Files
hide Files
:
2000293.pdf (Publisher version), 336KB
Name:
2000293.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2000293_Suppl.pdf (Supplementary material), 477KB
Name:
2000293_Suppl.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
http://pubs.acs.org/doi/pdf/10.1021/ja100645k (Publisher version)
Description:
-

Creators

show
hide
 Creators:
Chevelkov, V., Author
Xue, Y., Author
Linser, R.1, Author              
Skrynnikov, N. R., Author
Reif, B., Author
Affiliations:
1Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society, ou_1950286              

Content

show
hide
Free keywords: -
 Abstract: Analyses of solution 15N relaxation data and solid-state 1HN−15N dipolar couplings from a small globular protein, α-spectrin SH3 domain, produce a surprisingly similar pattern of order parameters. This result suggests that there is little or no ns−μs dynamics throughout most of the sequence and, in particular, in the structured portion of the backbone. At the same time, evidence of ns−μs motions is found in the flexible loops and termini. These findings, corroborated by the MD simulations of α-spectrin SH3 in a hydrated crystalline environment and in solution, are consistent with the picture of protein dynamics that has recently emerged from the solution studies employing residual dipolar couplings.

Details

show
hide
Language(s): eng - English
 Dates: 2010-03-192010-04-14
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1021/ja100645k
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of the American Chemical Society
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 132 (14) Sequence Number: - Start / End Page: 5015 - 5017 Identifier: -