Results 21 to 30 of about 448,472 (368)
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
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
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]
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
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
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]
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]
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.
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]
No ...
Sonia Longhi+6 more
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