Results 11 to 20 of about 1,883,575 (282)

Intrinsic structural disorder in cytoskeletal proteins. [PDF]

Cytoskeleton, 2013
Cytoskeleton, the internal scaffold of the cell, displays an exceptional combination of stability and dynamics. It is composed of three major filamentous networks, microfilaments (actin filaments), intermediate filaments (neurofilaments), and ...
Szabó, Beáta, Guharoy, Majnak, Martos, Sara Contreras, Tompa, Péter   +3 more
core   +6 more sources

Intrinsic Fluorescence of Intrinsically Disordered Proteins

, 2012
Resolution of the intrinsic emission properties of a protein by different fluorescence spectroscopy techniques is an invaluable tool to detect and characterize its structural architecture and conformational changes under different experimental conditions.
NEYROZ, PAOLO, Paolo Neyroz, Stefano Ciurli, CIURLI, STEFANO LUCIANO   +3 more
core   +3 more sources

Structural and functional studies of intrinsically disordered fibronectin-binding proteins [PDF]

, 2009
Bacterial fibronectin-binding proteins (FnBPs) mediate adhesion of bacteria to host tissues through binding to the human protein fibronectin (Fn). FnBPs are predicted to contain a series of intrinsically disordered Fn-binding repeats (FnBRs), which ...
Norris, Nicole Catherine
core   +6 more sources

Databases for intrinsically disordered proteins [PDF]

Acta Crystallographica Section D Structural Biology, 2022
Intrinsically disordered regions (IDRs) lacking a fixed three-dimensional protein structure are widespread and play a central role in cell regulation. Only a small fraction of IDRs have been functionally characterized, with heterogeneous experimental evidence that is largely buried in the literature.
Piovesan, Damiano, Monzon, Alexander Miguel, Quaglia, Federica, Tosatto, Silvio C. E.   +3 more
openaire   +2 more sources

Introducing Protein Intrinsic Disorder [PDF]

Chemical Reviews, 2014
Central to this model is the notion that the correct shape of the substrate can fit into the active site of the enzyme for enabling an efficient and specific catalysis, as observed for enzymes that hydrolyze β-but not α-glycosidic bonds. 1 Throughout the 20 th century, tens of thousands of structures have been solved and deposited in the Protein Data ...
Habchi, Johnny, Tompa, Peter, Longhi, Sonia, Uversky, Vladimir   +3 more
openaire   +4 more sources

Protein flexibility and intrinsic disorder [PDF]

Protein Science, 2004
AbstractComparisons were made among four categories of protein flexibility: (1) low‐B‐factor ordered regions, (2) high‐B‐factor ordered regions, (3) short disordered regions, and (4) long disordered regions. Amino acid compositions of the four categories were found to be significantly different from each other, with high‐B‐factor ordered and short ...
Radivojac, P., Obradovic, Z., Smith, DK, Zhu, G., Vucetic, S., Brown, CJ, Lawson, JD, Dunker, AK   +7 more
openaire   +4 more sources

MobiDB: intrinsically disordered proteins in 2021 [PDF]

Nucleic Acids Research, 2020
AbstractThe MobiDB database (URL: https://mobidb.org/) provides predictions and annotations for intrinsically disordered proteins. Here, we report recent developments implemented in MobiDB version 4, regarding the database format, with novel types of annotations and an improved update process.
Damiano Piovesan, Marco Necci, Nahuel Escobedo, Alexander Miguel Monzon, András Hatos, Ivan Micetic, Federica Quaglia, Lisanna Paladin, Pathmanaban Ramasamy, Zsuzsanna Dosztányi, Wim F. Vranken, Norman E. Davey, Gustavo D. Parisi, Mónika Fuxreiter, Silvio C. E. Tosatto   +14 more
openaire   +9 more sources

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

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, Debora Orcia, Wallace, B. A., Lopes, Jose Luiz S., Lopes, J.L.S., Ricardo DeMarco, Ana Paula U. Araujo, Orcia, D., B.A. Wallace, Jose Luiz S. Lopes, DeMarco, R.   +14 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