Results 11 to 20 of about 32,287 (136)

Ensemble Docking for Intrinsically Disordered Proteins. [PDF]

J Chem Inf Model
AbstractIntrinsically disordered proteins (IDPs) are implicated in many human diseases and are increasingly being pursued as drug targets. Conventional structure-based drug design methods that rely on well-defined binding sites are however, largely unsuitable for IDPs.
Dhar A, Sisk TR, Robustelli P.
europepmc   +3 more sources

Intrinsically disordered proteins [PDF]

Mol. BioSyst., 2012
Our understanding of protein function has been predominated by the view that proteins need to adopt a defined three dimensional structure to be able to carry out their function. Indeed, crystal structures of numerous proteins have been instrumental in establishing the structure– function paradigm.
Agnieszka, Dziedzic-Letka, Andrzej, Ozyhar   +1 more
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IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures

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
No ...
Habchi, Johnny, Tompa, Peter, Longhi, Sonia, Uversky, Vladimir   +3 more
openaire   +4 more sources

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

Intrinsically Disordered Proteins [PDF]

Cell, 2013
In the same way that neither a messy lab bench nor a clean one is a reliable indicator of a researcher’s productivity, a protein’s function cannot be judged solely on the basis of its neatly folded and stable domains. As evidenced by recent work discussed in this Select, we are learning that intrinsically disordered regions feature in many of the cell ...
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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, Gary A. Huber, Gary A. Huber, J. Andrew McCammon, J. Andrew McCammon   +4 more
doaj   +1 more source

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, Isabella C. Felli, Roberta Pierattelli   +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, Gábor Erdős, Pablo Mier, Gregorio Alanis-Lobato, Vasilis J. Promponas, Zsuzsanna Dosztányi, Miguel A. Andrade-Navarro   +6 more
doaj   +1 more source

NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences

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, Hiroki Amagai, Satoshi Fukuchi   +2 more
doaj   +1 more source