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.
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.
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 2004 JMB paper exploring how preformed structural elements in intrinsically disordered proteins (IDPs) facilitate efficient binding and partner recognition.
Notes on 2004 JMB paper exploring how preformed structural elements in intrinsically disordered proteins (IDPs) facilitate efficient binding and partner recognition.
Notes on 2013 PNAS paper introducing the role of charge distribution pattern (κ) in shaping IDP conformations. Highlights how linear charge segregation influences whether IDPs adopt random coil or compact, hairpin-like structures.
Notes on 2013 PNAS paper introducing the role of charge distribution pattern (κ) in shaping IDP conformations. Highlights how linear charge segregation influences whether IDPs adopt random coil or compact, hairpin-like structures.
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.
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.
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.
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 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.
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.
