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 and Harekrushna SAHOO

Basic information

Original name

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

Authors

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

Edition

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

Publisher

European Biophysics Journal, Springer Nature

Other information

Language

English

Type of outcome

Stať ve sborníku

Confidentiality degree

není předmětem státního či obchodního tajemství

Publication form

electronic version available online

References:

URL

DOI

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

Abstract

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.

Links

GF15-34684L, research and development project

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

Investor: Czech Science Foundation, Partner Agency (Austria)

LM2018140, large research infrastructures

Name: e-Infrastruktura CZ (Acronym: e-INFRA CZ)

Investor: Ministry of Education, Youth and Sports of the CR

Citovat

BERA, Krishnendu, Suchismita SUBADINI, Jozef HRITZ and 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, p. 1–226. Available from: 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 and 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, p.~1–226. Available from: https://dx.doi.org/10.1007/s00249-021-01558-w.

Detailed Information on Publication Record