Macromolecular crowding: how shape and interaction affect the structure, function, conformational dynamics and relative domain movement of a multi-domain protein
Author:
Affiliation:
1. Department of Chemistry, Indian Institute of Technology Kanpur, Kanpur-208 016, UP, India
Abstract
Funder
Science and Engineering Research Board
Council of Scientific and Industrial Research, India
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2022/CP/D1CP04842B
Reference108 articles.
1. Toward an understanding of biochemical equilibria within living cells
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3. Protein-complex stability in cells and in vitro under crowded conditions
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5. Macromolecular Crowding Tunes Folding Landscape of Parallel α/β Protein, Apoflavodoxin
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