2022
DOI: 10.1021/acsomega.2c06199
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Effects of External Perturbations on Protein Systems: A Microscopic View

Abstract: Protein folding can be viewed as the origami engineering of biology resulting from the long process of evolution. Even decades after its recognition, research efforts worldwide focus on demystifying molecular factors that underlie protein structure−function relationships; this is particularly relevant in the era of proteopathic disease. A complex co-occurrence of different physicochemical factors such as temperature, pressure, solvent, cosolvent, macromolecular crowding, confinement, and mutations that represe… Show more

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Cited by 8 publications
(1 citation statement)
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References 289 publications
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“…Protein-ligand interactions in crowded cellular environments play a crucial role in biological functions. [1][2][3] However, the crowded environment can perturb not only the overall protein structure and its fluctuations, [4][5][6][7][8] but also the local conformation, thereby influencing the binding pathway of protein-ligand reactions within the cellular milieu. [9][10][11] Recently, Feig et al used atomistic simulations to demonstrate that crowding can have diverse effects on enzyme function in vivo.…”
Section: Introductionmentioning
confidence: 99%
“…Protein-ligand interactions in crowded cellular environments play a crucial role in biological functions. [1][2][3] However, the crowded environment can perturb not only the overall protein structure and its fluctuations, [4][5][6][7][8] but also the local conformation, thereby influencing the binding pathway of protein-ligand reactions within the cellular milieu. [9][10][11] Recently, Feig et al used atomistic simulations to demonstrate that crowding can have diverse effects on enzyme function in vivo.…”
Section: Introductionmentioning
confidence: 99%