Impact of point mutations and amino acid modifications on the structure and stability of peptides and proteins probed by FT-IR spectroscopy

Download
  1. Get@NRC: Impact of point mutations and amino acid modifications on the structure and stability of peptides and proteins probed by FT-IR spectroscopy (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1016/0022-2860(95)08575-G
AuthorSearch for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for:
TypeArticle
Journal titleJournal of Molecular Structure
ISSN0022-2860
Volume348
Pages58; # of pages: 4
AbstractIR spectroscopy was used to study the impact of amino acid modifications on the association behaviour of β-amyloid peptides (βA4 peptides) and to investigate the effect of point mutations on the secondary structure of the enzyme ribonuclease T1 (RNase T1).
Publication date
PublisherElsevier B.V.
LanguageEnglish
AffiliationNational Research Council Canada; NRC Institute for Biodiagnostics
Peer reviewedYes
NRC number422
NPARC number9742644
Export citationExport as RIS
Report a correctionReport a correction
Record identifierba5e6681-ff02-476e-a9ec-3d37f8b4afce
Record created2009-07-17
Record modified2016-11-21
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)