Results 11 to 20 of about 1,786,374 (279)
Databases for intrinsically disordered proteins [PDF]
Acta Crystallographica Section D Structural Biology, 2022 Intrinsically disordered regions (IDRs) lacking a fixed three-dimensional protein structure are widespread and play a central role in cell regulation. Only a small fraction of IDRs have been functionally characterized, with heterogeneous experimental evidence that is largely buried in the literature.
Piovesan, Damiano +3 more
openaire +2 more sources
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
Introducing Protein Intrinsic Disorder [PDF]
Chemical Reviews, 2014 Central to this model is the notion that the correct shape of the substrate can fit into the active site of the enzyme for enabling an efficient and specific catalysis, as observed for enzymes that hydrolyze β-but not α-glycosidic bonds. 1 Throughout the 20 th century, tens of thousands of structures have been solved and deposited in the Protein Data ...
Habchi, Johnny +3 more
openaire +4 more sources
Protein flexibility and intrinsic disorder [PDF]
Protein Science, 2004 AbstractComparisons were made among four categories of protein flexibility: (1) low‐B‐factor ordered regions, (2) high‐B‐factor ordered regions, (3) short disordered regions, and (4) long disordered regions. Amino acid compositions of the four categories were found to be significantly different from each other, with high‐B‐factor ordered and short ...
Radivojac, P. +7 more
openaire +4 more sources
Investigating Intrinsically Disordered Proteins With Brownian Dynamics
Frontiers in Molecular Biosciences, 2022 Intrinsically disordered proteins (IDPs) have recently become systems of great interest due to their involvement in modulating many biological processes and their aggregation being implicated in many diseases.
Surl-Hee Ahn +4 more
doaj +1 more source
idpr: A package for profiling and analyzing Intrinsically Disordered Proteins in R
PLoS ONE, 2022 Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are proteins or protein-domains that do not have a single native structure, rather, they are a class of flexible peptides that can rapidly adopt multiple conformations ...
William M. McFadden, Judith L. Yanowitz
doaj +3 more sources
Adenoviral E1A Exploits Flexibility and Disorder to Target Cellular Proteins
Biomolecules, 2020 Direct interaction between intrinsically disordered proteins (IDPs) is often difficult to characterize hampering the elucidation of their binding mechanism.
Maria Grazia Murrali +2 more
doaj +1 more source
Evolutionary Study of Disorder in Protein Sequences
Biomolecules, 2020 Intrinsically disordered proteins (IDPs) contain regions lacking intrinsic globular structure (intrinsically disordered regions, IDRs). IDPs are present across the tree of life, with great variability of IDR type and frequency even between closely ...
Kristina Kastano +6 more
doaj +1 more source
MobiDB: intrinsically disordered proteins in 2021 [PDF]
Nucleic Acids Research, 2020 AbstractThe MobiDB database (URL: https://mobidb.org/) provides predictions and annotations for intrinsically disordered proteins. Here, we report recent developments implemented in MobiDB version 4, regarding the database format, with novel types of annotations and an improved update process.
Damiano Piovesan +14 more
openaire +9 more sources
Biophysics and Physicobiology, 2020 Intrinsically disordered proteins are those proteins with intrinsically disordered regions. One of the unique characteristics of intrinsically disordered proteins is the existence of functional segments in intrinsically disordered regions.
Hiroto Anbo +2 more
doaj +1 more source