Problems and caveats associated with the determination of protein conformation By FT-IR spectroscopy

Download
  1. Get@NRC: Problems and caveats associated with the determination of protein conformation By FT-IR spectroscopy (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1117/12.969611
AuthorSearch for: ; Search for: ; Search for: ; Search for: ; Search for:
TypeBook Chapter
Proceedings title7th Intl Conf on Fourier Transform Spectroscopy
Series titleSPIE Proceedings
Conference7th International Conference on Fourier Transform Spectroscopy, June 19, 1989, Fairfax, Virginia, USA
ISSN0277-786X
Volume1145
Pages580581
AbstractInfrared spectroscopy is being used increasingly to study the conformational structure of proteins and polypeptides in aqueous solution. The methodology generally used for the infrared spectroscopic analysis of protein secondary structure is based on three steps: 1. Separation of the overlapping amide I (amide C = O stretching) component bands via band-narrowing procedures such as Fourier self-deconvolution or derivation. 2. Assignment of the resolved component bands, based on previously established spectra-structure correlations, to different secondary structure elements, i.e., alpha helices, beta-sheets, turns or non-ordered conformations. 3. Extraction of quantitative information on protein secondary structure from analysis of amide I band profiles by curve fitting. Each of these three steps has potential sources of error which have to be recognized to prevent fallacious interpretations.
Publication date
PublisherSPIE
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedYes
NPARC number23001099
Export citationExport as RIS
Report a correctionReport a correction
Record identifier41f5648a-fc75-4cb5-b271-baa4fb547441
Record created2016-12-13
Record modified2016-12-13
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)