Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F15%3A00452032" target="_blank" >RIV/61388963:_____/15:00452032 - isvavai.cz</a>

Výsledek na webu

<a href="http://pubs.rsc.org/en/content/articlepdf/2015/cp/c5cp04475h" target="_blank" >http://pubs.rsc.org/en/content/articlepdf/2015/cp/c5cp04475h</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/c5cp04475h" target="_blank" >10.1039/c5cp04475h</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations

Popis výsledku v původním jazyce

We report a new multidimensional magic angle spinning NMR methodology, which provides an accurate and detailed probe of molecular motions occurring on timescales of nano- to microseconds, in sidechains of proteins. The approach is based on a 3D CPVC-RFDRcorrelation experiment recorded under fast MAS conditions (nu(R) = 62 kHz), where C-13-H-1 CPVC dipolar lineshapes are recorded in a chemical shift resolved manner. The power of the technique is demonstrated in model tripeptide Tyr-(D)Ala-Phe and two nano-crystalline proteins, GB1 and LC8. We demonstrate that, through numerical simulations of dipolar lineshapes of aromatic sidechains, their detailed dynamic profile, i.e., the motional modes, is obtained. In GB1 and LCH the results unequivocally indicate that a number of aromatic residues are dynamic, and using quantum mechanical calculations, we correlate the molecular motions of aromatic groups to their local environment in the crystal lattice. The approach presented here is general a

Název v anglickém jazyce

Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations

Popis výsledku anglicky

We report a new multidimensional magic angle spinning NMR methodology, which provides an accurate and detailed probe of molecular motions occurring on timescales of nano- to microseconds, in sidechains of proteins. The approach is based on a 3D CPVC-RFDRcorrelation experiment recorded under fast MAS conditions (nu(R) = 62 kHz), where C-13-H-1 CPVC dipolar lineshapes are recorded in a chemical shift resolved manner. The power of the technique is demonstrated in model tripeptide Tyr-(D)Ala-Phe and two nano-crystalline proteins, GB1 and LC8. We demonstrate that, through numerical simulations of dipolar lineshapes of aromatic sidechains, their detailed dynamic profile, i.e., the motional modes, is obtained. In GB1 and LCH the results unequivocally indicate that a number of aromatic residues are dynamic, and using quantum mechanical calculations, we correlate the molecular motions of aromatic groups to their local environment in the crystal lattice. The approach presented here is general a

Druh

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

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

—

Projekt

<a href="/cs/project/GA15-11223S" target="_blank" >GA15-11223S: Vodíkové vazby a nukleární kvantová delokalizace studované pomocí NMR spektroskopie a teoretických výpočtů</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Physical Chemistry Chemical Physics

ISSN

1463-9076

e-ISSN

—

Svazek periodika

17

Číslo periodika v rámci svazku

43

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

13

Strana od-do

28789-28801

Kód UT WoS článku

000364024100037

EID výsledku v databázi Scopus

2-s2.0-84946027409