Results 81 to 90 of about 7,902,914 (332)
Association/dissociation Mechanisms of Intrinsically Disordered Region of Protein Beyond Conformational Selection and Induced Fit [PDF]
We investigate association and dissociation mechanisms of a typical intrinsically disordered region (IDR), transcriptional activation subdomain of tumor repressor protein p53 (TAD-p53) with murine double-minute clone 2 protein (MDM2).
Duy Phuoc Tran (7400249) +3 more
core +1 more source
Intrinsic disorder and protein multibinding in domain, terminal, and linker regions [PDF]
Abstract Intrinsic disorder is believed to contribute to the ability of some proteins to interact with multiple partners which is important for protein functional promiscuity and regulation of the cross-talk between pathways.
Jessica H, Fong, Anna R, Panchenko
openaire +2 more sources
Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation
Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang +2 more
wiley +1 more source
Background: The evolutionary rate of disordered protein regions varies greatly due to the lack of structural constraints. So far, few studies have investigated the presence/absence patterns of compositional bias, indicative of disorder, across ...
Christos A. Ouzounis +3 more
doaj +1 more source
Unequivocal Single-Molecule Force Spectroscopy of Intrinsically Disordered Proteins [PDF]
Intrinsically disordered proteins (IDPs) are predicted to represent about one third of the eukaryotic proteome. The dynamic ensemble of conformations of this steadily growing class of proteins has remained hardly accessible for bulk biophysical ...
Rubén Hervás +12 more
core +1 more source
Emerging experimental and computational methods for studying redox‐regulated structural transitions
Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass +2 more
wiley +1 more source
Chaperone proteins are crucial for proper protein folding and quality control, especially when cells encounter stress caused by non-optimal temperatures. DnaK is one of such essential chaperones in bacteria. Although DnaK has been well characterized, the
Sirli Rosendahl +2 more
doaj +1 more source
Proteomimetic Strategy for the Modulation of Intrinsically Disordered Protein MYC
The difficulty in developing specific ligands for protein receptors is directly correlated to the presence of unique binding sites on the protein surface.
Thu Nguyen, Seong Ho Hong, P. Arora
semanticscholar +1 more source
Empirical predictions of an intrinsically disordered protein theory approach to glycan/lectin reaction kinetics [PDF]
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
Heterodimeric amino acid transporters consist of SLC7 and SLC3 family proteins arranged in a conserved structural organization. They regulate nutrient transport across cell membranes, supporting essential cellular functions. These transporters also contribute to xenobiotic/drug uptake and distribution.
Mariafrancesca Scalise +5 more
wiley +1 more source

