Results 101 to 110 of about 1,763,945 (204)
Eukaryotic proteins often feature long stretches of amino acids that lack a well-defined three-dimensional structure and are referred to as intrinsically disordered proteins (IDPs) or regions (IDRs).
Snigdha Maiti +4 more
doaj +1 more source
The two phosphorylation sites within the Gab1 fragment 142‐203 exhibit distinct structural characteristics. Tyr162 is in a disordered region, Y183 in a helical segment. ABSTRACT The biological function of intrinsically disordered proteins is frequently coupled to short linear motifs, which serve as protein binding sites.
Anne Dietrich +5 more
wiley +1 more source
Toward a consensus in protein structure nomenclature
In a recent article, published in Intrinsically Disordered Proteins, a valuable consensus view regarding the nomenclature for disordered proteins was presented.1 In this work the authors present a thoughtful and systemic review of terms that have been ...
DaSilva, Linder C +2 more
core +1 more source
Data–driven Modelling of Intrinsically Disordered Proteins [PDF]
In this thesis we investigated the relationships between amino acid sequence and biophysical properties of intrinsically disordered proteins involved in Parkinson's and Alzheimer's disease (IDPs), gauged from NMR ...
Tamiola, Kamil
core +1 more source
Programming Multidomain Peptides With Molecular Frustration Into Biomolecular Condensates
De novo designed multidomain peptides (MDPs) were used to explore how molecular ordering influences peptide phase behavior. MDPs containing partially folded β‐sheets were found to form biomolecular condensates. This work introduces a new design principle for condensate formation and expand the design space beyond conventional intrinsically disordered ...
Debdatta Das +12 more
wiley +1 more source
Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology
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.
Sravani Ramisetty +3 more
core +1 more source
Protein deep learning is moving from single structure prediction toward bound complex modeling and conformational ensemble generation. An architectural perspective shows how symmetry, evolutionary information, generative sampling, and energetic grounding shape performance and generalization.
Daniele Angioletti +3 more
wiley +1 more source
Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders [PDF]
The recent years have witnessed a rise in the number of intrinsically disor-dered proteins (IDPs), also known as hybrid proteins, which possess both struc-tured domains and biologically important intrinsically disordered protein regions (IDPRs).
Uversky, Vladimir N. +1 more
core +1 more source
Desiccation tolerance mechanisms in the green lineage and beyond
Ancient origin and recurrent evolution of desiccation tolerance in the green lineage. Summary Water is essential for life on Earth, yet some plants can survive the near‐complete loss of cellular water, a trait known as desiccation tolerance. Although rare in vegetative tissues of vascular plants, desiccation tolerance is scattered across the plant ...
Jenny Schuster, Robert VanBuren
wiley +1 more source
Charge interactions can dominate the dimensions of intrinsically disordered proteins [PDF]
Many eukaryotic proteins are disordered under physiological conditions, and fold into ordered structures only on binding to their cellular targets. Such intrinsically disordered proteins (IDPs) often contain a large fraction of charged amino acids. Here,
Nettels, D +23 more
core +1 more source

