Results 41 to 50 of about 40,484 (286)

Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics

Frontiers in Physics, 2019
Recognition of the natural abundance and functional importance of intrinsically disordered proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions (IDPRs) and ordered regions, is changing protein science.
Vladimir N. Uversky, Vladimir N. Uversky
doaj   +1 more source

Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology. [PDF]

PLoS ONE, 2013
The abundance and potential functional roles of intrinsically disordered regions in aquaporin-4, Kir4.1, a dystrophin isoforms Dp71, α-1 syntrophin, and α-dystrobrevin; i.e., proteins constituting the functional core of the astrocytic dystrophin ...
Insung Na, Derek Redmon, Markus Kopa, Yiru Qin, Bin Xue, Vladimir N Uversky   +5 more
doaj   +1 more source

Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology

Biomolecules, 2023
Intense study of intrinsically disordered proteins (IDPs) did not begin in earnest until the late 1990s when a few groups, working independently, convinced the community that these ‘weird’ proteins could have important functions.
Rachel Evans, Sravani Ramisetty, Prakash Kulkarni, Keith Weninger   +3 more
doaj   +1 more source

INTRINSIC PROTEIN DISORDER AND PROTEIN-PROTEIN INTERACTIONS [PDF]

Biocomputing 2012, 2011
Intrinsically disordered proteins often bind to more than one partner. In this study, we focused on 11 sets of complexes in which the same disordered segment becomes bound to two or more distinct partners. For this collection of protein complexes, two or more partners of each disordered segment were selected to have less than 25% amino acid identity ...
Wei-Lun Hsu, Christopher J. Oldfield, Jingwei Meng, Fei Huang, Bin Xue, Vladimir N. Uversky, Pedro Romero, A. Keith Dunker   +7 more
openaire   +2 more sources

Structural characterization of intrinsically disordered proteins by NMR spectroscopy.

, 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

Dss1 Is a 26S Proteasome Ubiquitin Receptor [PDF]

, 2014
The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Hardwick, Kevin G., Hay, Ronald T., Larsen, Ida B., Kragelund, Birthe B., Tatham, Michael H, Rösner, Heike I, Kragelund, Birthe Brandt, Hay, Ronald T, Kragelund, Birthe B, Kriegenburg, Franziska, Tatham, Michael H., Rösner, Heike Ilona, Paraskevopoulos, Konstantinos, Brandstrup, Rikke, Larsen, Ida B, Medina, Bethan; id_orcid, Hartmann-Petersen, Rasmus, Gordon, Colin, Rösner, Heike I., Hardwick, Kevin G, Medina, Bethan   +20 more
core   +1 more source

Expose flexible conformations for intrinsically disordered protein

Current Research in Structural Biology
The folding conformation of native protein has flexibility in different degrees, which may bring difficulty in presenting the structures, and also it causes complexity in understanding the relationship between structure and functions.
Jiaan Yang, Wenxin Ji, Wen Xiang Cheng, Gang Wu, Si Tong Sheng, Peng Zhang, Jun Lin, Xiaojia Chen, Qiong Shi   +8 more
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Conserved Outer Tegument Component UL11 from Herpes Simplex Virus 1 Is an Intrinsically Disordered, RNA-Binding Protein

mBio, 2020
A distinguishing morphological feature of all herpesviruses is the multiprotein tegument layer located between the nucleocapsid and lipid envelope of the virion. Tegument proteins play multiple roles in viral replication, including viral assembly, but we
Claire M. Metrick, Andrea L. Koenigsberg, Ekaterina E. Heldwein   +2 more
doaj   +1 more source

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

, 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

Proteins of generalist and specialist pathogens differ in their amino acid composition

Life Science Alliance, 2018
Primitive amino acids and disorder content in secreted proteins are distinctively enriched in generalist compared with host-specific pathogens. Pathogens differ in their host specificities, with species infecting a unique host (specialist pathogens) and ...
Luz P Blanco, Bryan L Payne, Felix Feyertag, David Alvarez-Ponce   +3 more
doaj   +1 more source