Results 71 to 80 of about 5,123 (214)
BMC Biology, 2023 Background Intrinsically disordered regions (IDRs) are widely distributed in proteins and related to many important biological functions. Accurately identifying IDRs is of great significance for protein structure and function analysis.
Yi-Jun Tang +4 more
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Biomolecules, 2021 Intrinsic disorder plays an important functional role in proteins. Disordered regions are linked to posttranslational modifications, conformational switching, extra/intracellular trafficking, and allosteric control, among other phenomena.
David Ortega-Alarcon +6 more
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Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain
, 2018 Herein, we describe a new series of fusion proteins that have been developed to self-assemble spontaneously into stable micelles that are 27 nm in diameter after enzymatic cleavage of a solubilizing protein tag. The sequences of the proteins are based on
Matthew, Francis +6 more
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Intrinsically Disordered Proteins (IDPs): Experimental and Computational Approaches in Drug Discovery [PDF]
Drug Designing & Intellectual Properties International Journal, 2018 Intrinsically disordered proteins (IDPs) are proteins that usually do not adopt well-defined native structures when isolated in solution under physiological conditions. Numerous IDPs have close relationships with human diseases such as Parkinson disease, Alzheimer disease, diabetes, and so on.
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Troubleshooting Guide to Expressing Intrinsically Disordered Proteins for Use in NMR Experiments
Frontiers in Molecular Biosciences, 2019 Intrinsically disordered proteins (IDPs) represent a structural class of proteins that do not have a well-defined, 3D fold in solution, and often have little secondary structure.
Steffen P. Graether
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Chemistry – A European Journal, EarlyView.ABSTRACT The rational design of hybrid nanomaterials with precisely controlled properties remains a central challenge in materials science. While atomically precise gold nanoclusters (Au‐NCs) offer molecule‐like control over a metallic core, tuning their optoelectronic behavior via surface engineering is often empirically driven.
Santiago Rodriguez +15 more
wiley +1 more source
AlphaFold2 models indicate that protein sequence determines both structure and dynamics
Scientific Reports, 2022 AlphaFold 2 (AF2) has placed Molecular Biology in a new era where we can visualize, analyze and interpret the structures and functions of all proteins solely from their primary sequences. We performed AF2 structure predictions for various protein systems,
Hao-Bo Guo +12 more
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Proteins: Structure, Function, and Bioinformatics, EarlyView.ABSTRACT The aggregation of human islet amyloid polypeptide (hIAPP) into cytotoxic oligomers and amyloid fibrils is a hallmark of type 2 diabetes mellitus (T2DM), leading to pancreatic β‐cell dysfunction. In contrast, rat IAPP (rIAPP) is largely non‐amyloidogenic. Osmolytes such as glucose, glycerol, and sorbitol are known to stabilize globular protein
Kiara A. Kidman +3 more
wiley +1 more source
NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions [PDF]
, 2020 Interactions of intrinsically disordered proteins are central to their cellular functions, and solution-state NMR spectroscopy provides a powerful tool for characterizing both structural and mechanistic aspects of such interactions.
Christodoulou, J +3 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