Results 71 to 80 of about 4,606,382 (149)
IDP-Bert: Predicting Properties of Intrinsically Disordered Proteins Using Large Language Models
The Journal of Physical Chemistry B22 pages, 5 ...
Parisa Mollaei +3 more
openaire +3 more sources
, 2020 Several intrinsically disordered proteins (IDPs) exhibit high affinity for lipid membranes. Among the different biophysical methods to probe protein-lipid interaction, neutron reflectometry (NR) can provide direct and structural detailed information on ...
Luchini A +5 more
core +1 more source
Prediction of Prion Proteins in E. coli Based on Bimodal Sequence Characteristics
Proteins: Structure, Function, and Bioinformatics, EarlyView.ABSTRACT Prions are infectious proteins that bear misfolded conformations capable of converting folded states into misfolded aggregates under physiologically relevant conditions. In mammals, prions cause deadly maladies including Creutzfeldt‐Jakob and chronic wasting disease. To date, several prion proteins have been identified in eukaryotes, primarily
Katherine Shreeve +5 more
wiley +1 more source
Role of charges in a dynamic disordered complex between an IDP and a folded domain
Nature CommunicationsProtein complexes involving intrinsically disordered proteins (IDPs) cover a continuum from IDPs that fully fold upon binding to IDPs that remain fully disordered in the complex. Here we demonstrate a case of charge-driven interactions of a folded domain
Katrine Bugge +10 more
doaj +1 more source
Dynamics of proteins with different molecular structures under solution condition
Scientific Reports, 2020 Incoherent quasielastic neutron scattering (iQENS) is a fascinating technique for investigating the internal dynamics of protein. However, low flux of neutron beam, low signal to noise ratio of QENS spectrometers and unavailability of well-established ...
Rintaro Inoue +12 more
doaj +1 more source
Insights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data [PDF]
, 2009 Background: Disordered proteins need to be expressed to carry out specified functions; however, their accumulation in the cell can potentially cause major problems through protein misfolding and aggregation.
Jones, DT +7 more
core +1 more source
PLOS ONE, 2015 Intrinsically disordered proteins (IDPs) are abundant in complex organisms. Due to their promiscuous nature and their ability to adopt several conformations IDPs constitute important points of network regulation. The family of Brain Expressed and X-linked (Bex) proteins consists of 5 members in humans (Bex1-5).
Fernandez, Eva M +2 more
openaire +5 more sources
Spatial Statistics for Screening Molecular Structures
Small, EarlyView.Deep architectures for materials discovery demand vast training data and obscure the structure‐property link. This review shows how spatial statistics offer a physically grounded alternative: voxelized fields and two‐point correlations, compressed by principal component analysis, yield convex, interpretable descriptors. Lean surrogates then reach sub‐2%
Pranoy Ray, Surya R. Kalidindi
wiley +1 more source
Structural investigation of Rett-inducing MeCP2 mutations
Genes and Diseases, 2019 X-ray structure of methyl-CpG binding domain (MBD) of MeCP2, an intrinsically disordered protein (IDP) involved in Rett syndrome, offers a rational basis for defining the spatial distribution for most of the sites where mutations responsible of Rett ...
Ottavia Spiga +6 more
doaj +1 more source
Empirical predictions of an intrinsically disordered protein theory approach to glycan/lectin reaction kinetics [PDF]
, 2012 Newly-developed methods from the theory of intrinsically disordered proteins can be applied to the flexible glycan structures that coat cellular surfaces and provide rich channels for biological information transmission.
Rodrick Wallace
core