Raman Spectroscopy of Proteins and Nucleoproteins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F13%3A10194636" target="_blank" >RIV/00216208:11320/13:10194636 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14740/13:00068311

Výsledek na webu

<a href="http://onlinelibrary.wiley.com/doi/10.1002/0471140864.ps1708s71/abstract" target="_blank" >http://onlinelibrary.wiley.com/doi/10.1002/0471140864.ps1708s71/abstract</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/0471140864.ps1708s71" target="_blank" >10.1002/0471140864.ps1708s71</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Raman Spectroscopy of Proteins and Nucleoproteins

Popis výsledku v původním jazyce

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 filamen

Název v anglickém jazyce

Raman Spectroscopy of Proteins and Nucleoproteins

Popis výsledku anglicky

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 filamen

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

<a href="/cs/project/GA202%2F09%2F0193" target="_blank" >GA202/09/0193: Vznik a dynamika strukturních motivů nukleových kyselin podílejících se na regulaci genové exprese</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Current Protocols in Protein Science

ISSN

1934-3655

e-ISSN

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Svazek periodika

71

Číslo periodika v rámci svazku

71:17.8.

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

52

Strana od-do

1-52

Kód UT WoS článku

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EID výsledku v databázi Scopus

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