Allostery

A modern view of allostery as an intrinsic property of protein dynamics, where conformational shifts, weak interactions, and energy landscapes enable regulation of function. Bridging classical models with cutting-edge experimental and theoretical insights, this review explores how proteins use dynamic ensembles and independent dynamic segments to facilitate signaling, folding, and ligand binding — redefining allostery beyond static views.

A modern view of allostery as an intrinsic property of protein dynamics, where conformational shifts, weak interactions, and energy landscapes enable regulation of function. Bridging classical models with cutting-edge experimental and theoretical insights, this review explores how proteins use dynamic ensembles and independent dynamic segments to facilitate signaling, folding, and ligand binding — redefining allostery beyond static views.

Notes on a 2003 Nature Structural Biology paper introducing the concept of evolutionarily conserved residue networks that mediate allosteric communication. Using sequence-based statistical coupling analysis (SCA), the authors map sparse, functionally critical networks in GPCRs, proteases, and hemoglobins, highlighting a fundamental mechanism of long-range communication in protein structures.

Notes on a 2003 Nature Structural Biology paper introducing the concept of evolutionarily conserved residue networks that mediate allosteric communication. Using sequence-based statistical coupling analysis (SCA), the authors map sparse, functionally critical networks in GPCRs, proteases, and hemoglobins, highlighting a fundamental mechanism of long-range communication in protein structures.

A 2010 Cell review expanding the classical models of protein-ligand binding to a dynamic landscape of conformational selection, induced fit, and independent dynamic segments. The paper highlights how ‘NOISE’—conformational fluctuations—can amplify signaling and regulate allosteric interactions, reshaping our understanding of binding and protein communication.

A 2010 Cell review expanding the classical models of protein-ligand binding to a dynamic landscape of conformational selection, induced fit, and independent dynamic segments. The paper highlights how ‘NOISE’—conformational fluctuations—can amplify signaling and regulate allosteric interactions, reshaping our understanding of binding and protein communication.

Notes on a 2014 PNAS paper analyzing PKA dynamics through community analysis.

Notes on 2010_PNAS study exploring how multisite phosphorylation of p53 modulates its interaction with CBP and transcriptional activation.

Notes on 2010_PNAS study exploring how multisite phosphorylation of p53 modulates its interaction with CBP and transcriptional activation.

Notes on 2010 Cell Review article exploring the structural and evolutionary principles that shape the dynamic regulatory mechanisms of protein kinases.

Notes on 2010 Cell Review article exploring the structural and evolutionary principles that shape the dynamic regulatory mechanisms of protein kinases.

Comprehensive review on how PKA holoenzyme assembly provides unique insights into kinase regulation, highlighting regulatory-catalytic subunit interactions, anchoring proteins, and macromolecular scaffolds.

Comprehensive review on how PKA holoenzyme assembly provides unique insights into kinase regulation, highlighting regulatory-catalytic subunit interactions, anchoring proteins, and macromolecular scaffolds.

A fascinating study revealing that TgCDPK1 is stabilized and activated via an allosteric mechanism involving its regulatory CAD domain, challenging classical models of calcium-dependent kinase activation.

A fascinating study revealing that TgCDPK1 is stabilized and activated via an allosteric mechanism involving its regulatory CAD domain, challenging classical models of calcium-dependent kinase activation.