Link to the University of Pittsburgh Homepage
Link to the University Library System Homepage Link to the Contact Us Form
D-Scholarship @ Pitt Banner and Links to Homepage

Sodium perchlorate effects on the helical stability of a mainly alanine peptide

Asciutto, EK and General, IJ and Xiong, K and Asher, SA and Madura, JD (2010) Sodium perchlorate effects on the helical stability of a mainly alanine peptide. Biophysical Journal, 98 (2). 186 - 196. ISSN 0006-3495

[img] Plain Text (licence)
Available under License : See the attached license file.
Download (1kB)

Abstract

Sodium perchlorate salt (NaClO4) is commonly used as an internal intensity standard in ultraviolet resonance Raman (UVRR) spectroscopy experiments. It is well known that NaClO4 can have profound effects on peptide stability. The impact of NaClO4 on protein stability in UVRR experiments has not yet been fully investigated. It is well known from experiment that protein stability is strongly affected by the solution composition (water, salts, osmolytes, etc.). Therefore, it is of the utmost importance to understand the physical basis on which the presence of salts and osmolytes in the solution impact protein structure and stability. The aim of this study is to investigate the effects of NaClO4, on the helical stability of an alanine peptide in water. Based upon replica-exchange molecular dynamics data, it was found that NaClO4 solution strongly stabilizes the helical state and that the number of pure helical conformations found at room temperature is greater than in pure water. A thorough investigation of the anion effects on the first and second solvation shells of the peptide, along with the Kirkwood-Buff theory for solutions, allows us to explain the physical mechanisms involved in the observed specific ion effects. A direct mechanism was found in which ClO4 ̄ ions are strongly attracted to the folded backbone. © 2010 by the Biophysical Society.

Share

Citation/Export:
Social Networking:
Share |

Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Asciutto, EK
General, IJ
Xiong, K
Asher, SAasher@pitt.eduASHER
Madura, JD
Date: 20 January 2010
Date Type: Publication
Journal or Publication Title: Biophysical Journal
Volume: 98
Number: 2
Page Range: 186 - 196
DOI or Unique Handle: 10.1016/j.bpj.2009.10.013
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 0006-3495
MeSH Headings: Alanine--chemistry; Algorithms; Circular Dichroism; Ions--chemistry; Models, Chemical; Peptides--chemistry; Perchloric Acid--chemistry; Protein Stability; Protein Structure, Secondary; Sodium Compounds--chemistry; Temperature; Water--chemistry
Other ID: NLM PMC2808484
PubMed Central ID: PMC2808484
PubMed ID: 20338840
Date Deposited: 08 Feb 2013 21:02
Last Modified: 12 Jun 2021 23:55
URI: http://d-scholarship-dev.library.pitt.edu/id/eprint/17241

Metrics

Monthly Views for the past 3 years

Plum Analytics

Altmetric.com

Actions (login required)

View Item View Item