The protein hydration layer in high glucose concentration: Dynamical responses in folded and intrinsically disordered dimeric states.

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Abstrakt

Tytuł:: The protein hydration layer in high glucose concentration: Dynamical responses in folded and intrinsically disordered dimeric states.
Autorzy:: Ghosh B; Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Kolkata, Mohanpur, 741 246, India.
Sengupta N; Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Kolkata, Mohanpur, 741 246, India. Electronic address: .
Źródło:: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2021 Nov 05; Vol. 577, pp. 124-129. Date of Electronic Publication: 2021 Sep 05.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Publication: <2002- >: San Diego, CA : Elsevier
Original Publication: New York, Academic Press.
MeSH Terms:: Molecular Dynamics Simulation*
Protein Folding*
Protein Multimerization*
Glucose/*chemistry
Intrinsically Disordered Proteins/*chemistry
Proteins/*chemistry
Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/metabolism ; Glucose/metabolism ; Hydrophobic and Hydrophilic Interactions ; Intrinsically Disordered Proteins/metabolism ; Protein Conformation ; Proteins/metabolism ; Ubiquitin/chemistry ; Ubiquitin/metabolism ; Water/chemistry
Contributed Indexing:: Keywords: Hydration water dynamics; Molecular crowder; Molecular dynamics; Protein conformation
Substance Nomenclature:: 0 (Amyloid beta-Peptides)
0 (Intrinsically Disordered Proteins)
0 (Proteins)
0 (Ubiquitin)
059QF0KO0R (Water)
IY9XDZ35W2 (Glucose)
Entry Date(s):: Date Created: 20210912 Date Completed: 20211126 Latest Revision: 20211126
Update Code:: 20240105
DOI:: 10.1016/j.bbrc.2021.09.005
PMID:: 34509724
: Czasopismo naukowe

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This exposition reveals the effect of glucose as a molecular crowder on the solvent environment in proximity of the protein surface in putative folded (Ubiquitin) and intrinsically disordered (dimeric Amyloid beta) states. Atomistic simulations reveal markedly higher structural perturbation in the disordered systems due to crowding effects, while the folded state retains overall structural fidelity. Key hydrophobic contacts in the disordered dimer are lost. However, glucose induced crowding results in elevated hydration on surfaces of both protein systems. Despite evident differences in their structural responses, the hydration layer of both the folded and disordered states display a distinct enhancement in lifetimes of mean residence and rotational relaxation under the hyperglycemic conditions. The results are crucial in the light of emergent co-solvent induced biological phenomena in crowded media.
Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Neelanjana Sengupta reports financial support was provided by Science and Engineering Research Board. Brataraj Ghosh reports financial support was provided by University Grants Commission.
(Copyright © 2021 Elsevier Inc. All rights reserved.)

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