Link to the University of Pittsburgh Homepage
Link to the University Library System Homepage Link to the Contact Us Form

UV resonance raman investigations of peptide and protein structure and dynamics

Oladepo, SA and Xiong, K and Hong, Z and Asher, SA and Handen, J and Lednev, IK (2012) UV resonance raman investigations of peptide and protein structure and dynamics. Chemical Reviews, 112 (5). 2604 - 2628. ISSN 0009-2665

[img] Plain Text (licence)
Available under License : See the attached license file.

Download (1kB)

Abstract

A study was conducted to demonstrate ultraviolet resonance Raman (UVRR) investigations of peptide and protein structure and dynamics. The tuning of the excitation wavelengths allowed the probing of different chromophoric segments of a macromolecule. Another advantage of deep UV Raman measurements was that there was no interference from molecular relaxed fluorescence, as those chromophores that had their first transition below 260 nm were highly flexible and possessed small fluorescence quantum yields. UVRR was also used in pump-probe measurements to give kinetic information on fast biological processes. It was a powerful technique for studying static protein structure and for studying protein dynamics, such as in protein folding. The rapid development of UVRR was aided by the latest advancements in lasers, optics, and detectors.


Share

Citation/Export:
Social Networking:
Share |

Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Oladepo, SA
Xiong, K
Hong, Z
Asher, SAasher@pitt.eduASHER
Handen, J
Lednev, IK
Date: 9 May 2012
Date Type: Publication
Journal or Publication Title: Chemical Reviews
Volume: 112
Number: 5
Page Range: 2604 - 2628
DOI or Unique Handle: 10.1021/cr200198a
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 0009-2665
Article Type: Review
MeSH Headings: Amino Acid Sequence; Amyloid--analysis; Bayes Theorem; Humans; Isotope Labeling; Kinetics; Models, Molecular; Molecular Sequence Data; Muramidase--analysis; Peptides--analysis; Protein Folding; Protein Structure, Secondary; Spectrum Analysis, Raman--instrumentation; Spectrum Analysis, Raman--methods; Thermodynamics; Vibration
Other ID: NLM NIHMS357786 [Available on 05/09/13], NLM PMC3349015 [Available on 05/09/13]
PubMed Central ID: PMC3349015
PubMed ID: 22335827
Date Deposited: 21 Feb 2013 22:50
Last Modified: 13 Oct 2017 18:56
URI: http://d-scholarship-dev.library.pitt.edu/id/eprint/17316

Metrics

Monthly Views for the past 3 years

Plum Analytics

Altmetric.com


Actions (login required)

View Item View Item