Results 31 to 40 of about 2,160,956 (299)
Intrinsically Disordered Energy Landscapes [PDF]
Scientific Reports, 2015 Abstract Analysis of an intrinsically disordered protein (IDP) reveals an underlying multifunnel structure for the energy landscape. We suggest that such ‘intrinsically disordered’ landscapes, with a number of very different competing low-energy structures, are likely to characterise IDPs and provide a useful way ...
Yassmine Chebaro +3 more
openaire +3 more sources
Exon-phase symmetry and intrinsic structural disorder promote modular evolution in the human genome [PDF]
, 2013 A key signature of module exchange in the genome is phase symmetry of exons, suggestive of exon shuffling events that occurred without disrupting translation reading frame.
Kalmár, Lajos +2 more
core +1 more source
Expanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs
Biomolecules, 2021 ErbBs are receptor tyrosine kinases involved not only in development, but also in a wide variety of diseases, particularly cancer. Their extracellular, transmembrane, juxtamembrane, and kinase folded domains were described extensively over the past 20 ...
Louise Pinet +2 more
doaj +1 more source
Buried and accessible surface area control intrinsic protein flexibility [PDF]
, 2013 Proteins experience a wide variety of conformational dynamics that can be crucial for facilitating their diverse functions. How is the intrinsic flexibility required for these motions encoded in their three-dimensional structures?
Marsh, Joseph A; id_orcid
core +1 more source
Critical assessment of protein intrinsic disorder prediction
, 2021 Intrinsically disordered proteins, defying the traditional protein structure–function paradigm, are a challenge to study experimentally. Because a large part of our knowledge rests on computational predictions, it is crucial that their accuracy is high ...
Necci, M +14 more
core +1 more source
Intrinsic Disorder and Functional Proteomics [PDF]
Biophysical Journal, 2007 The recent advances in the prediction of intrinsically disordered proteins and the use of protein disorder prediction in the fields of molecular biology and bioinformatics are reviewed here, especially with regard to protein function. First, a close look is taken at intrinsically disordered proteins and then at the methods used for their experimental ...
Radivojac, Predrag +5 more
openaire +3 more sources
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 +2 more
doaj +1 more source
Concentrating on intrinsic disorder [PDF]
Nature Reviews Molecular Cell Biology, 2018 Many eukaryotic proteins, including key transcription regulators, contain intrinsically disordered regions (IDRs), which serve as flexible interaction platforms. The molecular understanding of IDR-based interactions is now emerging, providing new insights into how IDRs promote protein compartmentalization and/or phase separation and how these processes
openaire +4 more sources
Frontiers in Physiology, 2013 The sodium dependent bicarbonate transporter NCBE/NBCn2 is predominantly expressed in the central nervous system (CNS). The highest protein abundance is found in the choroid plexus.
Kaare eBjerregaard-Andersen +7 more
doaj +1 more source
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 +14 more
core +2 more sources