Behavior of Intrinsically Disordered Proteins (IDPs) in Protein-Protein Complexes: Emphasis on Fuzziness

Notes on 2017 review discussing how intrinsically disordered proteins (IDPs) form various types of complexes including fuzzy complexes, with implications for flexible signaling and dynamic regulation.

Behavior of Intrinsically Disordered Proteins (IDPs) in Protein-Protein Complexes: Emphasis on Fuzziness

Notes on 2017 review discussing how intrinsically disordered proteins (IDPs) form various types of complexes including fuzzy complexes, with implications for flexible signaling and dynamic regulation.

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.

Anchor Residues in Protein–Protein Interactions

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.

Anchor Residues in Protein–Protein Interactions

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.

Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity

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.

Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity

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.

The Hallmark of AGC Kinase Functional Divergence is Its C-terminal Tail, a Cis-acting Regulatory Module

An elegant dissection of how the C-terminal tail (C-tail) in AGC kinases serves as a cis-acting regulatory module, driving functional divergence from other kinase families. Through conserved interactions and structural specialization, the C-tail orchestrates key regulatory processes, acting as a unique hallmark of AGC kinases.

The Hallmark of AGC Kinase Functional Divergence is Its C-terminal Tail, a Cis-acting Regulatory Module

An elegant dissection of how the C-terminal tail (C-tail) in AGC kinases serves as a cis-acting regulatory module, driving functional divergence from other kinase families. Through conserved interactions and structural specialization, the C-tail orchestrates key regulatory processes, acting as a unique hallmark of AGC kinases.

An Inherent Difference Between Serine and Threonine Phosphorylation: Phosphothreonine Strongly Prefers a Highly Ordered, Compact, Cyclic Conformation

Notes on 2023 ACS paper exploring structural differences between serine and threonine phosphorylation, focusing on phosphothreonine’s preference for ordered conformations.

An Inherent Difference Between Serine and Threonine Phosphorylation: Phosphothreonine Strongly Prefers a Highly Ordered, Compact, Cyclic Conformation

Notes on 2023 ACS paper exploring structural differences between serine and threonine phosphorylation, focusing on phosphothreonine’s preference for ordered conformations.

Architecture and Membrane Interaction of the EGF Receptor

A deep dive into the molecular dynamics and membrane interaction of EGFR, revealing distinct active and inactive conformations, the role of lipid environment, and subtle structural regulation.

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