NĚMEČEK, Daniel, Josef ŠTĚPÁNEK and George J. THOMAS. Raman Spectroscopy of Proteins and Nucleoproteins. Current Protocols in Protein Science. John Wiley & Sons, 2013, Neuveden, Suppl 71, p. "17.8.1"-"17.8.52", 52 pp. ISSN 1934-3655. Available from: https://dx.doi.org/10.1002/0471140864.ps1708s71.
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Basic information
Original name Raman Spectroscopy of Proteins and Nucleoproteins
Authors NĚMEČEK, Daniel (203 Czech Republic, guarantor, belonging to the institution), Josef ŠTĚPÁNEK (203 Czech Republic) and George J. THOMAS (840 United States of America).
Edition Current Protocols in Protein Science, John Wiley & Sons, 2013, 1934-3655.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14740/13:00068311
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1002/0471140864.ps1708s71
Keywords in English viral protein; virus assembly; DNA recognition; Raman spectroscopy
Tags ok, rivok
Tags International impact, Reviewed
Changed by Changed by: Olga Křížová, učo 56639. Changed: 11/4/2014 14:38.
Abstract
A protein Raman spectrum comprises discrete bands representing vibrational modes of the peptide backbone and its side chains. The spectral positions, intensities, and polarizations of the Raman bands are sensitive to protein secondary, tertiary, and quaternary structures and to side-chain orientations and local environments. In favorable cases, the Raman spectrum serves as an empirical signature of protein three-dimensional structure, intramolecular dynamics, and intermolecular interactions. Quantitative analysis of Raman spectral series can be further boosted by advanced statistical approaches of factor analysis that allow fitting of specific theoretical models while reducing the amount of analyzed data. Here, the strengths of Raman spectroscopy are illustrated by considering recent applications from the authors’ work that address (1) subunit folding and recognition in assembly of the icosahedral bacteriophages, (2) orientations of subunit main chains and side chains in native filamentous viruses, (3) roles of cysteine hydrogen bonding in the folding, assembly, and function of virus structural proteins, and (4) structural determinants of protein/DNA recognition in gene regulatory complexes. Conventional Raman and polarized Raman techniques are surveyed.
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