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Piezoelectric allostery of protein

Physical Review E, 2016
Allostery is indispensable for a protein to work, where a locally applied stimulus is transmitted to a distant part of the molecule. While the allostery due to chemical stimuli such as ligand binding has long been studied, the growing interest in mechanobiology prompts the study of the mechanically stimulated allostery, the physical mechanism of which ...
Jun, Ohnuki   +2 more
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Allostery in enzyme catalysis

Current Opinion in Structural Biology, 2017
Modern interpretations of allostery typically rely on conformational ensembles to describe enzyme function. Conformational motions controlling these ensembles are often stimulated or quenched by allosteric effectors, and are critical to optimizing ligand binding pockets and enzyme architectures.
George P, Lisi, J Patrick, Loria
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Review: Allostery in Chaperonins

Journal of Structural Biology, 2001
Chaperonins mediate protein folding in an ATP-dependent manner. ATP binding and hydrolysis by chaperonins are subject to both homotropic and heterotropic allosteric regulation. In the case of GroEL and CCT, homotropic regulation by ATP is manifested in nested cooperativity, which involves positive intra-ring cooperativity and negative inter-ring ...
A, Horovitz   +3 more
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A Chemical Perspective on Allostery

Chemical Reviews, 2016
Much work has been done in the past decade to quantify the phenomenon of allosteric communication in proteins. Every new study unveils an extra piece of the puzzle in our search for an understanding of allostery that allows us to make predictions on the response of a protein to medically relevant stimuli such as pathological mutations or drug binding ...
Andre A S T, Ribeiro, Vanessa, Ortiz
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Allostery in Drug Development

2019
Allosteric regulation is a ubiquitous strategy employed in nature to control cellular processes by regulating the affinities of biomolecules. Allosteric modulators are able to tune the protein/substrate affinity in a highly predictable way, suggesting that such modulators may represent safe drugs.
Xi, Cheng, Hualiang, Jiang
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Allostery in chaperonins

Rendiconti Lincei, 2006
Chaperonins mediate protein folding in an ATP-dependent manner. ATP binding and hydrolysis by chaperonins are subject to both homotropic and heterotropic allosteric regulation. In the case of GroEL and CCT, homotropic regulation by ATP is manifested in nested cooperativity, which involves positive intra-ring cooperativity and negative inter-ring ...
Amnon Horovitz   +3 more
openaire   +1 more source

Allostery and the lac Operon

Journal of Molecular Biology, 2013
The ability to regulate gene expression is essential for controlling metabolic events in a cell. Proteins that function like molecular switches respond to fluctuations in the environment to maintain homeostasis. The operon model, proposed by Jacob and Monod, provides a cogent depiction for how gene expression is regulated. A molecular mechanism for the
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A trailing ribosome speeds up RNA polymerase at the expense of transcript fidelity via force and allostery

Cell, 2023
Liang Meng Wee   +2 more
exaly  

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