Results 41 to 50 of about 11,653 (194)
Allostery vs. “allokairy” [PDF]
Proceedings of the National Academy of Sciences, 2015 A hallmark feature of biological systems is that they are tightly regulated. Whether it is turning genes on and off, controlling cell division, or tuning the activity of enzymes, nature has evolved an intricate array of regulatory measures to ensure that systems can optimally respond to the myriad of environmental queues that determine everything from ...
Vincent J, Hilser +2 more
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Protein allostery. computational characterization of diguanylate cyclase PleD [PDF]
, 2009 In biology, accurate cellular regulation in response to environmental signals is crucial for the fitness of organisms. On the molecular level the modulation of protein activity is often achieved by the binding of a signaling molecule or by covalent ...
Schmid, Franziska F.-F.
core +1 more source
PLoS Biology, 2013 Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distinct site. There is growing evidence that allosteric cooperativity can be communicated by modulation of protein dynamics without conformational change ...
Thomas L Rodgers +8 more
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Mechanisms of DNA-mediated allostery
, 2023 Proteins often regulate their activities via allostery - or action at a distance - in which the binding of a ligand at one binding site influences the affinity for another ligand at a distal site.
Carlon, Enrico +3 more
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Frontiers in Molecular Biosciences, 2023 Mesophilic and thermophilic enzyme counterparts are often studied to understand how proteins function under harsh conditions. To function well outside of standard temperature ranges, thermophiles often tightly regulate their structural ensemble through ...
Alexa L. Knight +2 more
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Quarterly Reviews of BiophysicsAbstract Allostery describes the ability of biological macromolecules to transmit signals spatially through the molecule from an allosteric site – a site that is distinct from orthosteric binding sites of primary, endogenous ligands – to the functional or active site.
Mateu Montserrat-Canals +2 more
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Long-Range Signaling in MutS and MSH Homologs via Switching of Dynamic Communication Pathways. [PDF]
PLoS Computational Biology, 2016 Allostery is conformation regulation by propagating a signal from one site to another distal site. This study focuses on the long-range communication in DNA mismatch repair proteins MutS and its homologs where intramolecular signaling has to travel over ...
Beibei Wang +5 more
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Evidence of variable human Fcγ receptor-Fc affinities across differentially-complexed IgG
mAbs, 2023 Antibody-mediated effector functions are widely considered to unfold according to an associative model of IgG-Fcγ receptor (FcγR) interactions. The associative model presupposes that Fc receptors cannot discriminate antigen-bound IgG from free IgG in ...
Andrew R. Crowley +5 more
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Frontiers in Molecular Biosciences, 2020 The allosteric effect is one of the most important processes in regulating the function of proteins, and the elucidation of this phenomenon plays a significant role in understanding emergent behaviors in biological regulation.
Giovanni Villani
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Heterotropic regulation and negative homotropic cooperativity
FEBS Open Bio, EarlyView.We identified a structural module common to some proteins that couple negative cooperativity with heterotropic regulation, two features that rarely coexist. These proteins are ring‐like and present an ordered asymmetry whereby noncontacting subunits are symmetric, and their tertiary structure differs from that of contacting subunits.
Veronica Morea +5 more
wiley +1 more source