Results 121 to 130 of about 3,579,241 (217)
Intrinsically disordered proteins studied by NMR spectroscopy
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of complex multi-domain proteins are now identified as a trend topic by the scientific community.
Marco Schiavina +7 more
doaj +1 more source
Thermoresponsive intrinsically disordered protein polymers
Thermoresponsive intrinsically disordered protein polymers (TIDPPs) are a unique class of biopolymers that lack a fixed three-dimensional structure under physiological conditions and exhibit temperature-responsive behavior. These properties are primarily
Uversky, Vladimir N. +2 more
core +1 more source
Adaptation of the bound intrinsically disordered protein YAP to mutations at the YAP:TEAD interface
Many interactions between proteins are mediated by intrinsically disordered regions (IDRs). Intrinsically disordered proteins (IDPs) do not adopt a stable three-dimensional structure in their unbound form, but they become more structured upon binding to ...
Fontana, Patrizia (author) +10 more
core +1 more source
The conformational ensemble and function of intrinsically disordered proteins (IDPs) are sensitive to their solution environment. The inherent malleability of disordered proteins, combined with the exposure of their residues, accounts for this ...
Shraddha KC +9 more
doaj +1 more source
Electrostatics in intrinsically disordered proteins
Protein-protein interactions are fundamental to many biological processes. A large proportion of proteins have been identified as partially or entirely disordered in their native state.
Wong, Eric Tsz Chung
core +1 more source
Accurate Generation of Conformational Ensembles for Intrinsically Disordered Proteins with IDPFold
Intrinsically disordered proteins (IDPs) play pivotal roles in various biological functions whose dynamic structures are closely associated with many human diseases, including cancer, diabetes, and Alzheimer disease.
Junjie Zhu +10 more
doaj +1 more source
Computational identification and analysis of protein short linear motifs
Short linear motifs (SLiMs) in proteins can act as targets for proteolytic cleavage, sites of post-translational modification, determinants of sub-cellular localization, and mediators of protein-protein interactions.
Davey, Norman E. +2 more
core +1 more source
Residue-level coarse-grained (CG) molecular dynamics (MD) simulation is widely used to investigate slow biological processes that involve multiple proteins, nucleic acids, and their complexes. Biomolecules in a large simulation system are distributed non-
Jaewoon Jung, Cheng Tan, Yuji Sugita
doaj +1 more source
Abstract Self-organization of multicellular systems is vital for building structure in living system but remains underexplored in engineered living materials. We developed iDP 2 , a platform enabling high-density display of intrinsically disordered proteins on the surface of
Rong Chang, Hann Tu, Neel S. Joshi
openaire +1 more source
Beyond the structure-function paradigm: A comprehensive review of intrinsically disordered proteins. [PDF]
Harake SNA +4 more
europepmc +1 more source

