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.
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.
Notes on 2004 PNAS paper introducing the concept of anchor residues as key pre-configured side chains that drive protein–protein interactions. The study highlights a two-step binding mechanism, combining preformed ‘anchor’ interactions and induced-fit adjustments.
Notes on 2004 PNAS paper introducing the concept of anchor residues as key pre-configured side chains that drive protein–protein interactions. The study highlights a two-step binding mechanism, combining preformed ‘anchor’ interactions and induced-fit adjustments.
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 the 2001 JMB paper introducing SOCKET, a computational tool that identifies coiled-coil motifs based on structural features rather than sequence patterns. Highlights the diversity of coiled-coil structures, the central role of knobs-into-holes packing, and applications in structural analysis and design.
Notes on the 2001 JMB paper introducing SOCKET, a computational tool that identifies coiled-coil motifs based on structural features rather than sequence patterns. Highlights the diversity of coiled-coil structures, the central role of knobs-into-holes packing, and applications in structural analysis and design.
Notes on a landmark Nature (1999) paper detailing how calmodulin (CaM) adopts a unique binding mode when interacting with CaMKK, revealing an extended 26-residue peptide interface and an opposite binding orientation, distinguishing it from classical CaM-target interactions — a new paradigm in calcium signaling complexes.
Notes on a landmark Nature (1999) paper detailing how calmodulin (CaM) adopts a unique binding mode when interacting with CaMKK, revealing an extended 26-residue peptide interface and an opposite binding orientation, distinguishing it from classical CaM-target interactions — a new paradigm in calcium signaling complexes.
