Results 31 to 40 of about 40,484 (286)
Protein structure is determined by the amino acid sequence and a variety of post-translational modifications, and provides the basis for physiological properties.
Akshatha Ganne +7 more
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Protein intrinsic disorder in plants
To some extent contradicting the classical paradigm of the relationship between protein 3D structure and function, now it is clear that large portions of the proteomes, especially in higher organisms, lack a fixed structure and still perform very important functions.
Pazos, Florencio +3 more
openaire +4 more sources
Intrinsically Disordered Proteins and the Janus Challenge
To gain a new insight into the role of proteins in the origin of life on Earth, we present the Janus Challenge: identify an intrinsically disordered protein (IDP), naturally occurring or synthetic, that has catalytic activity.
Prakash Kulkarni, Vladimir N. Uversky
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Inferring function using patterns of native disorder in proteins [PDF]
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
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Function, Regulation, and Dysfunction of Intrinsically Disordered Proteins
The discovery that a considerable fraction of the eukaryotic proteins lacks a well-defined three-dimensional structure in their native state has revolutionised our general understanding of proteins [...]
Giuliana Fusco, Stefano Gianni
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New insights into disordered proteins and regions according to the FOD-M model.
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 +3 more
doaj +2 more sources
Intrinsically Disordered Proteins in Neurodegeneration [PDF]
Intrinsically disordered proteins (IDPs) have gained wide recognition due to their versatile roles in cell physiology and pathology. A large repertoire of IDPs has been implicated in numerous diseases, making them potential targets for therapeutic intervention.
openaire +2 more sources
Conformational Recognition of an Intrinsically Disordered Protein [PDF]
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. +7 more
openaire +3 more sources
Differences in the number of intrinsically disordered regions between yeast duplicated proteins, and their relationship with functional divergence. [PDF]
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 +2 more
doaj +1 more source
DisProt in 2024: improving function annotation of intrinsically disordered proteins [PDF]
International audienceDisProt (URL: https://disprot.org) is the gold standard database for intrinsically disordered proteins and regions, providing valuable information about their functions. The latest version of DisProt brings significant advancements,
Longhi, Sonia +81 more
core +1 more source

