Vibrational circular dichroism study of solvent- and temperature-induced conformational changes in poly-gamma-benzyl-L-glutamate and poly-beta-benzyl-L-aspartate

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F13%3A43895079" target="_blank" >RIV/60461373:22340/13:43895079 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.vibspec.2013.01.007" target="_blank" >http://dx.doi.org/10.1016/j.vibspec.2013.01.007</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.vibspec.2013.01.007" target="_blank" >10.1016/j.vibspec.2013.01.007</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Vibrational circular dichroism study of solvent- and temperature-induced conformational changes in poly-gamma-benzyl-L-glutamate and poly-beta-benzyl-L-aspartate

Popis výsledku v původním jazyce

Vibrational circular dichroism (VCD) spectroscopy was used to study the effect of the different composition of mixed solvents and temperature on the conformation and aggregation states of two synthetically prepared polypeptides, poly-gamma-benzyl-L-glutamate (PBLG) and poly-beta-benzyl-L-aspartate (PBLA). Additions of trifluoroacetic acid (TFA) into a solution of heligenic solvents trichloromethane and benzene-d6 caused the conformational change from the alpha-helical to polyproline II-like for both ofthe polypeptides, which represented interesting transition previously mostly observed in aqueous solutions rather than in organic solvents. The VCD method proved a lower stability of the alpha-helical conformation of PBLA than PBLG and the structural differences between these polypeptides. The variation of temperature in the region 13-50 degrees C induced atypical conformational transformations in the PBLG/trichloromethane/TFA and PBLG/benzene-d6/TFA systems. The usually more stable alph

Název v anglickém jazyce

Vibrational circular dichroism study of solvent- and temperature-induced conformational changes in poly-gamma-benzyl-L-glutamate and poly-beta-benzyl-L-aspartate

Popis výsledku anglicky

Vibrational circular dichroism (VCD) spectroscopy was used to study the effect of the different composition of mixed solvents and temperature on the conformation and aggregation states of two synthetically prepared polypeptides, poly-gamma-benzyl-L-glutamate (PBLG) and poly-beta-benzyl-L-aspartate (PBLA). Additions of trifluoroacetic acid (TFA) into a solution of heligenic solvents trichloromethane and benzene-d6 caused the conformational change from the alpha-helical to polyproline II-like for both ofthe polypeptides, which represented interesting transition previously mostly observed in aqueous solutions rather than in organic solvents. The VCD method proved a lower stability of the alpha-helical conformation of PBLA than PBLG and the structural differences between these polypeptides. The variation of temperature in the region 13-50 degrees C induced atypical conformational transformations in the PBLG/trichloromethane/TFA and PBLG/benzene-d6/TFA systems. The usually more stable alph

Druh

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

CEP obor

CB - Analytická chemie, separace

OECD FORD obor

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Projekt

<a href="/cs/project/GAP208%2F11%2F0105" target="_blank" >GAP208/11/0105: Rozšíření metod vibrační optické aktivity pro oblast biomolekul</a><br>

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

Vibrational Spectroscopy

ISSN

0924-2031

e-ISSN

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Svazek periodika

66

Číslo periodika v rámci svazku

neuvedeno

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

1-7

Kód UT WoS článku

000319097100001

EID výsledku v databázi Scopus

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