Perturbing the unfolding of CRABP I using polyethylene glycol:
An experimental and theoretical study

D 2021

Perturbing the unfolding of CRABP I using polyethylene glycol: An experimental and theoretical study

BERA, Krishnendu, Suchismita SUBADINI, Jozef HRITZ a Harekrushna SAHOO

Základní údaje

Originální název

Perturbing the unfolding of CRABP I using polyethylene glycol: An experimental and theoretical study

Autoři

BERA, Krishnendu, Suchismita SUBADINI, Jozef HRITZ a Harekrushna SAHOO

Vydání

13th EBSA congress, July 24–28, 2021, Vienna, Austria, od s. 1–226, 2021

Nakladatel

European Biophysics Journal, Springer Nature

Další údaje

Jazyk

angličtina

Typ výsledku

Stať ve sborníku

Utajení

není předmětem státního či obchodního tajemství

Forma vydání

elektronická verze "online"

Odkazy

URL

DOI

http://dx.doi.org/10.1007/s00249-021-01558-w

Příznaky

Mezinárodní význam

Změněno: 30. 9. 2021 00:34, Krishnendu Bera, Ph.D.

Anotace

V originále

Proteins significantly affected by crowding nature of macromolecules. Thus, it is pertinent to investigate the role of crowding environment on the denaturation and renaturation kinetics of protein. Different molecular weights of Polyethylene glycol (PEG) have been considered as a molecular crowders and CRABP I (cellular retinoic acid binding protein I),as a model protein in this study. The secondary structure analysis was performed by circular dichroism (CD) spectroscopy and the unfolding kinetics using intrinsic fluorescence of CRABP I at 37o C to mimic the in vivo condition. Both PEG 2000 and PEG 4000 act as stabilizers by hamstring the unfolding kinetic rates. The unfolding kinetic slopes were different for both PEG, which indicating PEG favour compact conformations of protein as a function of concentration and molecular weight. The molecular dynamics(MD) studies revealed that PEG 2000 molecules assembled together during the 500 ns simulation, which is increasing the stability and percentage of β-sheet of the protein. The experimental findings were well supported by the theoretical results.

Návaznosti

GF15-34684L, projekt VaV

Název: Efektivní výpočty volných energií a konfiguračního vzorkování protein-‐proteinových interakcí

Investor: Grantová agentura ČR, Efektivní výpočty volných energií a konfiguračního vzorkování protein-proteinových interakcí, Partnerská agentura (Rakousko)

LM2018140, velká výzkumná infrastruktura

Název: e-Infrastruktura CZ (Akronym: e-INFRA CZ)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, e-Infrastruktura CZ

Citovat

BERA, Krishnendu, Suchismita SUBADINI, Jozef HRITZ a Harekrushna SAHOO. Perturbing the unfolding of CRABP I using polyethylene glycol: An experimental and theoretical study. Online. In 13th EBSA congress, July 24–28, 2021, Vienna, Austria. European Biophysics Journal, Springer Nature, 2021, s. 1–226. Dostupné z: https://dx.doi.org/10.1007/s00249-021-01558-w.

@inproceedings{1784138,
   author = {Bera, Krishnendu and Subadini, Suchismita and Hritz, Jozef and Sahoo, Harekrushna},
   booktitle = {13th EBSA congress, July 24–28, 2021, Vienna, Austria},
   doi = {http://dx.doi.org/10.1007/s00249-021-01558-w},
   howpublished = {elektronická verze "online"},
   language = {eng},
   pages = {1–226},
   publisher = {European Biophysics Journal, Springer Nature},
   title = {Perturbing the unfolding of CRABP I using polyethylene glycol: An experimental and theoretical study},
   url = {https://link.springer.com/journal/249/volumes-and-issues/50-1/supplement},
   year = {2021}
}

TY  - JOUR
ID  - 1784138
AU  - Bera, Krishnendu - Subadini, Suchismita - Hritz, Jozef - Sahoo, Harekrushna
PY  - 2021
TI  - Perturbing the unfolding of CRABP I using polyethylene glycol: An experimental and theoretical study
PB  - European Biophysics Journal, Springer Nature
UR  - https://link.springer.com/journal/249/volumes-and-issues/50-1/supplement
N2  - Proteins significantly affected by crowding nature of macromolecules. Thus, it is pertinent to investigate the role of crowding environment on the denaturation and renaturation kinetics of protein. Different molecular weights of Polyethylene glycol (PEG) have been considered as a molecular crowders and CRABP I (cellular retinoic acid binding protein I),as a model protein in this study. The secondary structure analysis was performed by circular dichroism (CD) spectroscopy and the unfolding kinetics using intrinsic fluorescence of CRABP I at 37o C to mimic the in vivo condition. Both PEG 2000 and PEG 4000 act as stabilizers by hamstring the unfolding kinetic rates. The unfolding kinetic slopes were different for both PEG, which indicating PEG favour compact conformations of protein as a function of concentration and molecular weight. The molecular dynamics(MD) studies revealed that PEG 2000 molecules assembled together during the 500 ns simulation, which is increasing the stability and percentage of β-sheet of the protein. The experimental findings were well supported by the theoretical results.
ER  -

BERA, Krishnendu, Suchismita SUBADINI, Jozef HRITZ a Harekrushna SAHOO. Perturbing the unfolding of CRABP I using polyethylene glycol: An experimental and theoretical study. Online. In \textit{13th EBSA congress, July 24–28, 2021, Vienna, Austria}. European Biophysics Journal, Springer Nature, 2021, s.~1–226. Dostupné z: https://dx.doi.org/10.1007/s00249-021-01558-w.

Podrobný výpis o publikaci