Raman Spectroscopy of Proteins and Nucleoproteins

J 2013

Raman Spectroscopy of Proteins and Nucleoproteins

NĚMEČEK, Daniel; Josef ŠTĚPÁNEK a George J. THOMAS

Základní údaje

Originální název

Raman Spectroscopy of Proteins and Nucleoproteins

Autoři

NĚMEČEK, Daniel (203 Česká republika, garant, domácí); Josef ŠTĚPÁNEK (203 Česká republika) a George J. THOMAS (840 Spojené státy)

Vydání

Current Protocols in Protein Science, John Wiley & Sons, 2013, 1934-3655

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Kód RIV

RIV/00216224:14740/13:00068311

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1002/0471140864.ps1708s71

Klíčová slova anglicky

viral protein; virus assembly; DNA recognition; Raman spectroscopy

Štítky

ok, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 11. 4. 2014 14:38, Olga Křížová

Anotace

V originále

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.

Citovat

NĚMEČEK, Daniel; Josef ŠTĚPÁNEK a George J. THOMAS. Raman Spectroscopy of Proteins and Nucleoproteins. Current Protocols in Protein Science. John Wiley & Sons, 2013, Neuveden, Suppl 71, s. "17.8.1"-"17.8.52", 52 s. ISSN 1934-3655. Dostupné z: https://dx.doi.org/10.1002/0471140864.ps1708s71.

@article{1107002,
   author = {Němeček, Daniel and Štěpánek, Josef and Thomas, George J.},
   article_number = {Suppl 71},
   doi = {http://dx.doi.org/10.1002/0471140864.ps1708s71},
   keywords = {viral protein; virus assembly; DNA recognition; Raman spectroscopy},
   language = {eng},
   issn = {1934-3655},
   journal = {Current Protocols in Protein Science},
   title = {Raman Spectroscopy of Proteins and Nucleoproteins},
   volume = {Neuveden},
   year = {2013}
}

TY  - JOUR
ID  - 1107002
AU  - Němeček, Daniel - Štěpánek, Josef - Thomas, George J.
PY  - 2013
TI  - Raman Spectroscopy of Proteins and Nucleoproteins
JF  - Current Protocols in Protein Science
VL  - Neuveden
IS  - Suppl 71
SP  - "17.8.1"-"17.8.52"
EP  - "17.8.1"-"17.8.52"
PB  - John Wiley & Sons
SN  - 19343655
KW  - viral protein
KW  - virus assembly
KW  - DNA recognition
KW  - Raman spectroscopy
N2  - 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.
ER  -

NĚMEČEK, Daniel; Josef ŠTĚPÁNEK a George J. THOMAS. Raman Spectroscopy of Proteins and Nucleoproteins. \textit{Current Protocols in Protein Science}. John Wiley \&{} Sons, 2013, Neuveden, Suppl 71, s.~''17.8.1''-''17.8.52'', 52 s. ISSN~1934-3655. Dostupné z: https://dx.doi.org/10.1002/0471140864.ps1708s71.

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