Results 21 to 30 of about 1,786,374 (279)

Structural characterization of intrinsically disordered proteins by NMR spectroscopy. [PDF]

, 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 ...
Contreras-Martos, Sara, Peter Tompa, Cedeno, Cesyen, Simone Kosol, Kosol, Simone, Tompa, Péter, Sara Contreras-Martos, Cesyen Cedeño   +7 more
core   +1 more source

Polycation-π Interactions Are a Driving Force for Molecular Recognition by an Intrinsically Disordered Oncoprotein Family [PDF]

, 2013
Molecular recognition by intrinsically disordered proteins (IDPs) commonly involves specific localized contacts and target-induced disorder to order transitions.
Sheung Chun Ng, Ng Sheung Chun, Hue Sun Chan (135066), Chan, Hue Sun, Song Jianhui, Song, Jianhui, Jianhui Song, Tompa, Péter, Lee Kevin A. W., Peter Tompa, Lee, Kevin Andrew William, Sheung Chun Ng (463510), Jianhui Song (463509), Tompa Peter, Hue Sun Chan, Peter Tompa (38445), Chan Hue Sun, Ng, Sheung Chun, Kevin A. W. Lee (7686), Kevin A W Lee   +19 more
core   +1 more source

Fairy tails: Flexibility and function of intrinsically disordered extensions in the photosynthetic world

Frontiers in Molecular Biosciences, 2015
Intrinsically Disordered Proteins (IDPs), or protein fragments also called Intrinsically Disordered Regions (IDRs), display high flexibility as the result of their amino acid composition. They can adopt multiple roles.
Gabriel eThieulin-Pardo, Luisana eAvilan, Mila eKojadinovic, Brigitte eGontero   +3 more
doaj   +1 more source

Open questions: Reflections on intrinsically disordered proteins [PDF]

Network Biology, 2021
Intrinsically Disordered Proteins or Regions (IDPs) are proteins that lack a predetermined 3D structure playing key cellular functions including regulation, signaling, and protein-protein/DNA interaction.
Mouna Choura, Ahmed Rebai
doaj  

Ensemble Docking for Intrinsically Disordered Proteins. [PDF]

J Chem Inf Model
Abstract Intrinsically 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   +4 more sources

Folding factors and partners for the intrinsically disordered protein Micro-Exon Gene 14 (MEG-14) [PDF]

, 2013
The micro-exon genes (MEG) of Schistosoma mansoni, a parasite responsible for the second most widely spread tropical disease, code for small secreted proteins with sequences unique to the Schistosoma genera.
Orcia, Debora, Araujo, A.P.U., Wallace, Bonnie A., Araújo, Ana Paula Ulian de, De Marco, Ricardo, Araujo, Ana Paula U., Debora Orcia, Wallace, B. A., Lopes, Jose Luiz S., DeMarco, Ricardo, Lopes, J.L.S., Ricardo DeMarco, Ana Paula U. Araujo, Orcia, D., B.A. Wallace, Wallace, B.A., Jose Luiz S. Lopes, DeMarco, R.   +17 more
core   +1 more source

DisBind: A database of classified functional binding sites in disordered and structured regions of intrinsically disordered proteins

BMC Bioinformatics, 2017
Background Intrinsically unstructured or disordered proteins function via interacting with other molecules. Annotation of these binding sites is the first step for mapping functional impact of genetic variants in coding regions of human and other genomes,
Jia-Feng Yu, Xiang-Hua Dou, Yu-Jie Sha, Chun-Ling Wang, Hong-Bo Wang, Yi-Ting Chen, Feng Zhang, Yaoqi Zhou, Ji-Hua Wang   +8 more
doaj   +1 more source

Insights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data [PDF]

, 2009
Background: Disordered proteins need to be expressed to carry out specified functions; however, their accumulation in the cell can potentially cause major problems through protein misfolding and aggregation.
Edwards, Y.J.K., Jones, DT, Pentony, MM, Jones, D.T., Edwards, YJK, Lobley, A.E., Pentony, M.M., David T Jones, Yvonne JK Edwards, Lobley, AE, Anna E Lobley, Melissa M Pentony   +11 more
core   +1 more source

Intrinsically disordered proteins: modes of binding with emphasis on disordered domains

Open Biology, 2021
Our notions of protein function have long been determined by the protein structure–function paradigm. However, the idea that protein function is dictated by a prerequisite complementarity of shapes at the binding interface is becoming increasingly ...
Owen Michael Morris, James Hilary Torpey, Rivka Leah Isaacson   +2 more
doaj   +1 more source

Intrinsic disorder in putative protein sequences [PDF]

Proteome Science, 2011
Intrinsically disordered proteins (IDPs) and regions (IDRs) perform a variety of crucial biological functions despite lacking stable tertiary structure under physiological conditions in vitro. State-of-the-art sequence-based predictors of intrinsic disorder are achieving per-residue accuracies over 80%.
Uros Midic, Zoran Obradovic
openaire   +3 more sources