Results 41 to 50 of about 1,786,374 (279)

Differences in the number of intrinsically disordered regions between yeast duplicated proteins, and their relationship with functional divergence. [PDF]

PLoS ONE, 2011
BACKGROUND: Intrinsically disordered regions are enriched in short interaction motifs that play a critical role in many protein-protein interactions. Since new short interaction motifs may easily evolve, they have the potential to rapidly change protein ...
Floriane Montanari, Denis C Shields, Nora Khaldi   +2 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   +3 more sources

[Intrinsically disordered proteins]. [PDF]

Postepy biochemii, 2012
Intrinsically disordered proteins (IDPs) belong to the newly discovered and still growing group of proteins. In contrast to globular proteins IDPs fail to fold into a well-defined tertiary structure under physiological conditions and they are characterized by extraordinary structural flexibility and plasticity.
Agnieszka, Dziedzic-Letka, Andrzej, Ozyhar   +1 more
  +6 more sources

New insights into disordered proteins and regions according to the FOD-M model

PLoS ONE, 2022
A collection of intrinsically disordered proteins (IDPs) having regions with the status of intrinsically disordered (IDR) according to the Disprot database was analyzed from the point of view of the structure of hydrophobic core in the structural unit ...
Irena Roterman, Katarzyna Stapor, Piotr Fabian, Leszek Konieczny   +3 more
doaj   +2 more sources

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

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

Conformational Recognition of an Intrinsically Disordered Protein [PDF]

Biophysical Journal, 2014
There is a growing interest in understanding the properties of intrinsically disordered proteins (IDPs); however, the characterization of these states remains an open challenge. IDPs appear to have functional roles that diverge from those of folded proteins and revolve around their ability to act as hubs for protein-protein interactions.
Krieger J. M., Fusco G., Lewitzky M., Simister P. C., Marchant J., Camilloni C., Feller S. M., De Simone A.   +7 more
openaire   +3 more sources

Inferring function using patterns of native disorder in proteins [PDF]

, 2007
Natively unstructured regions are a common feature of eukaryotic proteomes. Between 30% and 60% of proteins are predicted to contain long stretches of disordered residues, and not only have many of these regions been confirmed experimentally, but they ...
Swindells, MB, Jones, DT, Mark B. Swindells, David T. Jones, Lobley, A, Lobley, A., Christine A. Orengo, David T Jones, Mark B Swindells, Swindells, M.B., Orengo, C.A., Christine A Orengo, Jones, D.T., Anna Lobley, Orengo, CA   +14 more
core   +2 more sources

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
doaj   +1 more source