Notes on 2000 Proteins paper introducing the concept of ’natively unfolded’ proteins and how charge and hydrophobicity dictate their intrinsic disorder under physiological conditions.
Notes on 2000 Proteins paper introducing the concept of ’natively unfolded’ proteins and how charge and hydrophobicity dictate their intrinsic disorder under physiological conditions.
Notes on a 2002 Trends in Cell Biology review introducing phosphorylation-specific prolyl isomerization as a novel signaling mechanism. Pin1-mediated cis-trans switching of pSer/Thr-Pro motifs acts as a conformational timer for cellular signaling, impacting activity, interactions, and localization of key regulatory proteins.
Notes on a 2002 Trends in Cell Biology review introducing phosphorylation-specific prolyl isomerization as a novel signaling mechanism. Pin1-mediated cis-trans switching of pSer/Thr-Pro motifs acts as a conformational timer for cellular signaling, impacting activity, interactions, and localization of key regulatory proteins.
Notes on 2014 Cell paper that identifies the ‘DFG+1’ residue as a key determinant of Ser/Thr kinase phosphoacceptor specificity, with structural and biochemical validation.
Notes on 2014 Cell paper that identifies the ‘DFG+1’ residue as a key determinant of Ser/Thr kinase phosphoacceptor specificity, with structural and biochemical validation.
A groundbreaking exploration of how sequence patterning, especially proline and charge distributions, governs the conformational behavior of intrinsically disordered regions (IDRs) even under multisite phosphorylation, with compensatory conformational changes maintaining overall dimensions.
A groundbreaking exploration of how sequence patterning, especially proline and charge distributions, governs the conformational behavior of intrinsically disordered regions (IDRs) even under multisite phosphorylation, with compensatory conformational changes maintaining overall dimensions.
A groundbreaking study connecting protein folding energy landscapes to functional conformational changes in signaling proteins, showing how transient, non-native hydrogen bonds lower transition barriers and facilitate activation without unfolding.
A groundbreaking study connecting protein folding energy landscapes to functional conformational changes in signaling proteins, showing how transient, non-native hydrogen bonds lower transition barriers and facilitate activation without unfolding.
Notes on 2023 ACS paper exploring structural differences between serine and threonine phosphorylation, focusing on phosphothreonine’s preference for ordered conformations.
Notes on 2023 ACS paper exploring structural differences between serine and threonine phosphorylation, focusing on phosphothreonine’s preference for ordered conformations.
A detailed analysis of Rhodopsin Kinase (RK) autophosphorylation sites and their functional implications, highlighting purification strategies and structural analysis using proteolysis and mass spectrometry.
A detailed analysis of Rhodopsin Kinase (RK) autophosphorylation sites and their functional implications, highlighting purification strategies and structural analysis using proteolysis and mass spectrometry.
An in-depth review of CaMKK signaling, including structural, regulatory, and functional insights into its activation, downstream effects, and implications for disease.
