English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Interpretation of Amide I Difference Bands Observed during Protein Reactions Using Site-Directed Isotopically Labeled Bacteriorhodopsin as a Model System

Hauser, K., Engelhard, M., Friedman, N., Sheves, M., & Siebert, F. (2002). Interpretation of Amide I Difference Bands Observed during Protein Reactions Using Site-Directed Isotopically Labeled Bacteriorhodopsin as a Model System. Journal of Physical Chemistry A, 106(14): 1, pp. 3553-3559. Retrieved from http://dx.doi.org/10.1021/jp012926e.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : J. Phys. Chem. A

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Hauser, Karin, Author
Engelhard, Martin1, Author           
Friedman, Noga, Author
Sheves, Mordechai, Author
Siebert, Friedrich, Author
Affiliations:
1Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              

Content

show
hide
Free keywords: -
 Abstract: Reaction-induced infrared difference spectra show characteristic amide I spectral changes, which indicate conformational changes of the protein backbone but which cannot be interpreted at a molecular level. To obtain sonic insights into their causes, we used bacteriorhodopsin as a model system and investigated its BR --> N transition during which the largest amide I changes are observed. For the molecular interpretation, we labeled a single peptide C=O group at specific positions of the backbone with C-13 and monitored the resulting isotope effects. This has been achieved by replacing specific amino acids with a cysteine. Because wild-type bacteriorhodopsin does not contain this amino acid, (1-C- 13)cysteine can be incorporated into the mutants for site- directed isotopic labeling. Although the isotope-induced spectral changes are very small, we observed clear isotope effects for the middle to extracellular part of helices B, C, and F, indicating that the backbone of these parts of the protein is distorted during the reaction, whereas no label effects could be identified for the E-F loop and for the cytosolic regions of helices E and F. The results are discussed within the framework of recent experimental and theoretical studies of the amide I band, and they are correlated to the structural changes observed by other methods.

Details

show
hide
Language(s): eng - English
 Dates: 2002-04-11
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 18130
URI: http://dx.doi.org/10.1021/jp012926e
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Physical Chemistry A
  Alternative Title : J. Phys. Chem. A
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 106 (14) Sequence Number: 1 Start / End Page: 3553 - 3559 Identifier: -