Results 171 to 180 of about 18,737 (212)
Some of the next articles are maybe not open access.
Hemoglobin allostery and pharmacology
Molecular Aspects of Medicine, 2022The oxygen demands of the human body require the constant circulation of blood carrying an enormous concentration of hemoglobin (Hb). Oxygen transport depends not only on the amount of Hb, but also on the control over the affinity of the protein for the gas, which can be optimized for the environmental conditions by changes in the concentration of ...
Andrea Bellelli, Jeremy R.H. Tame
openaire +2 more sources
Allostery and cooperativity revisited [PDF]
Protein Science, 2008 Abstract Although phenomenlogical models that account for cooperativity in allosteric systems date back to the early and mid‐60's (e.g., the KNF and MWC models), there is resurgent interest in the topic due to the recent experimental and computational studies that attempted to reveal, at an atomistic level, how allostery actually ...
Qiang Cui
exaly +3 more sources
Protein topology and allostery
Current Opinion in Structural Biology, 2020Allostery plays important roles in many biological processes. Although all non-fibrous proteins may be allosteric, currently only a limited number of allosteric proteins are known. How allosteric regulation depends on protein topology and what are the preferred folds in allosteric proteins need to be explored.
Juan, Xie, Luhua, Lai
openaire +2 more sources
Correlating allostery with rigidity
Mol. BioSyst., 2011Allosteric proteins demonstrate the phenomenon of a ligand binding to a protein at a regulatory or effector site and thereby changing the chemical affinity of the catalytic site. As such, allostery is extremely important biologically as a regulatory mechanism for molecular concentrations in many cellular processes.
A J, Rader, Stephen M, Brown
openaire +2 more sources
Review: Allostery in Chaperonins
Journal of Structural Biology, 2001Chaperonins 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
openaire +2 more sources
Piezoelectric allostery of protein
Physical Review E, 2016Allostery 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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
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