Monitoring the Secondary Structure of Proteins by Near-Infrared Spectroscopy
Abstract:Despite the numerous applications of near-infrared spectroscopy in the agricultural and bio-industrial sectors, the relevance of this technique to the study of the secondary structure of proteins has received little attention. The present research investigated the near-infrared spectra of 12 model proteins in the solid state by taking the corresponding mid-infrared data into account. The second-derivative spectra of myoglobin, beta-lactoglobulin, and beta -casein in the near-infrared region revealed characteristic absorption bands. While myoglobin presented absorption bands at 2055, 2170, 2289, and 2350 nm, beta-lactoglobulin exhibited specific peaks at 2203, 2267, and 2300 nm. The second-derivative spectrum of beta-casein showed a particularly intense band at 2269 nm. The results derived from a generalized canonical correlation analysis confirmed the potential of near-infrared spectroscopy to characterize the secondary structure of proteins: 2172 and 2289 nm appeared to be representative of alpha-helix structure; 2205, 2264, and 2313 nm were observed for beta sheet; 2265 nm characterized the unordered structure.
Document Type: Research Article
Publication date: February 1, 1999
More about this publication?
- The Society publishes the internationally recognized, peer reviewed journal, Applied Spectroscopy, which is available both in print and online. Subscriptions are included with membership or can be purchased by institutional or corporate organizations. Abstracts may be viewed free of charge. Previously published as Bulletin (Society for Applied Spectroscopy)
- Editorial Board
- Information for Authors
- Submit a Paper
- Subscribe to this Title
- Membership Information
- Request copyrighted SAS materials
- Spectroscopic Nomenclature
- Focal Point (Open Access)
- ingentaconnect is not responsible for the content or availability of external websites