Crowding by Poly(ethylene glycol) Destabilizes Chemotaxis Protein Y (CheY)-Reference-Cited by-同舟云学术

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Crowding by Poly(ethylene glycol) Destabilizes Chemotaxis Protein Y (CheY)

Published:2022-07-07 Issue:14 Volume:61 Page:1431-1443
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Irukuvajjula Shivkumar Sharma¹^ORCID,Reddy Jithender G.²,Vadrevu Ramakrishna¹^ORCID

Affiliation:

1. Department of Biological Sciences, Birla Institute of Technology & Science─Pilani, Hyderabad Campus, Jawahar Nagar, Shamirpet, Hyderabad 500078, India

2. NMR Division, Department of Analytical & Structural Chemistry, CSIR-Indian Institute of Chemical Technology, Ministry of Science and Technology, Uppal Road, Tarnaka, Hyderabad 500007, India

Funder

Science and Engineering Research Board

Department of Science and Technology, Ministry of Science and Technology, India

Birla Institute of Technology and Science, Pilani

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.2c00030

Reference90 articles.

1. Principles that Govern the Folding of Protein Chains

2. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli

3. Macromolecular Crowding: Biochemical, Biophysical, and Physiological Consequences

4. Macromolecular crowding: obvious but underappreciated

5. Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli

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1. PEG-mCherry interactions beyond classical macromolecular crowding;2024-05-07

2. Polyethylene Glycol Impacts Conformation and Dynamics of Escherichia coli Prolyl-tRNA Synthetase Via Crowding and Confinement Effects;Biochemistry;2024-04-12

3. Studying protein stability in crowded environments by NMR;Progress in Nuclear Magnetic Resonance Spectroscopy;2024-04

4. Bridging Soft Interaction and Excluded Volume in Crowded Milieu through Subtle Protein Dynamics;The Journal of Physical Chemistry B;2024-01-16

5. Towards the energy landscape of adenylate kinase in crowded milieu: Activity, conformation, structure and dynamics in sequence;Archives of Biochemistry and Biophysics;2023-07

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