Water-Membrane Partition Thermodynamics of an Amphiphilic Lipopeptide: An Enthalpy-Driven Hydrophobic Effect

Notes on 2008 Biophysical Journal paper analyzing the thermodynamics of membrane insertion for an H-ras lipopeptide anchor (ANCH), highlighting the role of enthalpy-driven hydrophobic effects and conformational selection.

Water-Membrane Partition Thermodynamics of an Amphiphilic Lipopeptide: An Enthalpy-Driven Hydrophobic Effect

Notes on 2008 Biophysical Journal paper analyzing the thermodynamics of membrane insertion for an H-ras lipopeptide anchor (ANCH), highlighting the role of enthalpy-driven hydrophobic effects and conformational selection.

Preformed Structural Elements Feature in Partner Recognition by Intrinsically Unstructured Proteins

Notes on 2004 JMB paper exploring how preformed structural elements in intrinsically disordered proteins (IDPs) facilitate efficient binding and partner recognition.

Preformed Structural Elements Feature in Partner Recognition by Intrinsically Unstructured Proteins

Notes on 2004 JMB paper exploring how preformed structural elements in intrinsically disordered proteins (IDPs) facilitate efficient binding and partner recognition.

Diversity of Conformational States and Changes within the EF-hand Protein Superfamily

Notes on a 1999 Proteins review analyzing the conformational diversity of EF-hand motifs in calcium-binding proteins. Introduces Vector Geometry Mapping (VGM) to dissect helix movements beyond simple interhelical angles, and discusses functional implications of EF-hand plasticity.

Diversity of Conformational States and Changes within the EF-hand Protein Superfamily

Notes on a 1999 Proteins review analyzing the conformational diversity of EF-hand motifs in calcium-binding proteins. Introduces Vector Geometry Mapping (VGM) to dissect helix movements beyond simple interhelical angles, and discusses functional implications of EF-hand plasticity.

Net Charge Per Residue Modulates Conformational Ensembles of Intrinsically Disordered Proteins

Notes on 2010 PNAS paper exploring how net charge per residue (NCPR) governs the balance between collapsed and extended conformations in intrinsically disordered proteins (IDPs), with implications for understanding IDP behavior and function.

Net Charge Per Residue Modulates Conformational Ensembles of Intrinsically Disordered Proteins

Notes on 2010 PNAS paper exploring how net charge per residue (NCPR) governs the balance between collapsed and extended conformations in intrinsically disordered proteins (IDPs), with implications for understanding IDP behavior and function.

The Changing Landscape of Protein Allostery: Dynamic Ensembles and Functional Shifts

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.

The Changing Landscape of Protein Allostery: Dynamic Ensembles and Functional Shifts

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.

Binding Mechanism of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment

Comprehensive 2016 Frontiers review on the diverse binding mechanisms of intrinsically disordered proteins (IDPs), covering theory, simulations, and experimental insights into how disorder facilitates interaction dynamics, specificity, and versatility in cellular signaling.

Binding Mechanism of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment

Comprehensive 2016 Frontiers review on the diverse binding mechanisms of intrinsically disordered proteins (IDPs), covering theory, simulations, and experimental insights into how disorder facilitates interaction dynamics, specificity, and versatility in cellular signaling.

Induced Fit, Conformational Selection, and Independent Dynamic Segments: An Extended View of Binding Events

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.

Induced Fit, Conformational Selection, and Independent Dynamic Segments: An Extended View of Binding Events

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.

DFGmodel: Predicting Protein Kinase Structure in Inactive States for Structure-based Discovery of Type-II Inhibitors

Notes on 2014 ACS paper introducing DFGmodel, a computational approach to predict kinase inactive structures for type-II inhibitor discovery. Includes insights on DFG-flip and kinase conformational analysis.

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