Results 21 to 30 of about 448,472 (368)

IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures

open access: yesBMC 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

Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry

open access: yesChemical Reviews, 2022
Motions in biomolecules are critical for biochemical reactions. In cells, many biochemical reactions are executed inside of biomolecular condensates formed by ultradynamic intrinsically disordered proteins.
A. Abyzov   +2 more
semanticscholar   +1 more source

Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range

open access: yesbioRxiv, 2022
The formation and viscoelastic properties of condensates of intrinsically disordered proteins (IDPs) is dictated by amino acid sequence and solution conditions.
Giulio Tesei, K. Lindorff-Larsen
semanticscholar   +1 more source

Intrinsically disordered proteins [PDF]

open access: yesMol. 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.
Kyou-Hoon Han, Peter Tompa, Peter Tompa
openaire   +3 more sources

idpr: A package for profiling and analyzing Intrinsically Disordered Proteins in R

open access: yesPLoS 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   +2 more sources

NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins

open access: yesChemical Reviews, 2022
Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing essential roles in all aspects of cellular and extracellular biochemistry.
Aldo R. Camacho-Zarco   +9 more
semanticscholar   +1 more source

Protein intrinsic disorder in plants [PDF]

open access: yesFrontiers in Plant Science, 2013
To some extent contradicting the classical paradigm of the relationship between protein 3D structure and function, now it is clear that large portions of the proteomes, especially in higher organisms, lack a fixed structure and still perform very important functions.
Pazos, Florencio   +3 more
openaire   +4 more sources

Membrane shape deformation induced by curvature-inducing proteins consisting of chiral crescent binding and intrinsically disordered domains [PDF]

open access: yesJ. Chem. Phys. 157, 034901 (2022), 2022
Curvature-inducing proteins containing a Bin/Amphiphysin/Rvs domain often have intrinsically disordered domains. Recent experiments have shown that these disordered chains enhance curvature sensing and generation. Here, we report on the modification of protein-membrane interactions by disordered chains using meshless membrane simulations.
arxiv   +1 more source

Intrinsically Disordered Proteins: Critical Components of the Wetware.

open access: yesChemical Reviews, 2022
Despite the wealth of knowledge gained about intrinsically disordered proteins (IDPs) since their discovery, there are several aspects that remain unexplored and, hence, poorly understood.
Prakash Kulkarni   +9 more
semanticscholar   +1 more source

Introducing Protein Intrinsic Disorder [PDF]

open access: yesChemical Reviews, 2014
No ...
Sonia Longhi   +6 more
openaire   +6 more sources

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