Results 11 to 20 of about 1,763,945 (204)
Brain Expressed and X-Linked (Bex) Proteins Are Intrinsically Disordered Proteins (IDPs) and Form New Signaling Hubs [PDF]
PLoS ONE, 2015 Intrinsically disordered proteins (IDPs) are abundant in complex organisms. Due to their promiscuous nature and their ability to adopt several conformations IDPs constitute important points of network regulation. The family of Brain Expressed and X-linked (Bex) proteins consists of 5 members in humans (Bex1-5).
Marcal Vilar
exaly +7 more sources
Biomolecules, 2022 Research in previous decades has shown that intrinsically disordered proteins (IDPs) and regions in proteins (IDRs) are as ubiquitous as highly ordered proteins. Despite this, research on IDPs and IDRs still has many gaps left to fill.
Miloš Avramov +7 more
doaj +2 more sources
Structural Characterization of Intrinsically Disordered Proteins by NMR Spectroscopy [PDF]
Molecules, 2013 Recent advances in NMR methodology and techniques allow the structural investigation of biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well-suited for the study of intrinsically disordered proteins (IDPs) and ...
Peter Tompa +3 more
doaj +2 more sources
Intrinsically disordered proteins: controlled chaos or random walk [PDF]
International Journal of Plant Biology, 2016 Traditional conventions that a protein’s sequence dictates its definitive, tertiary structure, and that this fixed structure provides the protein with the ability to carry out its designated role(s) are still correct but not for all proteins.
T.C. Howton +3 more
doaj +2 more sources
Intrinsically disordered proteins (IDPs) in trypanosomatids. [PDF]
BMC Genomics, 2014 Proteins are composed of one or more amino acid chains and exhibit several structure levels. IDPs (intrinsically disordered proteins) represent a class of proteins that do not fold into any particular conformation and exist as dynamic ensembles in their native state.
de Cássia Ruy P +5 more
europepmc +4 more sources
Structural and functional studies of intrinsically disordered fibronectin-binding proteins [PDF]
, 2009 Bacterial fibronectin-binding proteins (FnBPs) mediate adhesion of bacteria to host tissues through binding to the human protein fibronectin (Fn). FnBPs are predicted to contain a series of intrinsically disordered Fn-binding repeats (FnBRs), which ...
Norris, Nicole Catherine
core +6 more sources
Frontiers in Aging Neuroscience, 2022 Protein structure is determined by the amino acid sequence and a variety of post-translational modifications, and provides the basis for physiological properties.
Akshatha Ganne +7 more
doaj +1 more source
BMC Molecular and Cell Biology, 2022 Background Intrinsically disordered proteins (IDPs) lack a stable three-dimensional structure under physiological conditions but play crucial roles in many biological processes.
CanZhuang Sun, YongE Feng, GuoLiang Fan
doaj +1 more source
Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins
Biomolecules, 2021 Single molecule fluorescence and nuclear magnetic resonance spectroscopy (NMR) are two very powerful techniques for the analysis of intrinsically disordered proteins (IDPs).
Samuel Naudi-Fabra +2 more
doaj +1 more source
Structural Analysis of Intrinsically Disordered Protein (IDP): TRIOBP [PDF]
Biophysical Journal, 2014 TRIOBP is an actin-bundling protein. Mutations of TRIOBP are associated with human deafness DFNB28. TRIOBP has three isoforms, named TRIOBP-1, TRIOBP-4, and TRIOBP-5. In vitro, TRIOBP isoform 4 (TRIOBP-4) forms dense F-actin bundles resembling the inner ear hair cell rootlet structure.
Gunther, Laura K. +4 more
openaire +1 more source