Results 171 to 180 of about 5,123 (214)

Hybrid deep learning with protein language models and dual-path architecture for predicting IDP functions. [PDF]

Brief Bioinform
Liang J, Luo Y, Su B, Peng Z.
europepmc   +1 more source

New Approach for Targeting Small-Molecule Candidates for Intrinsically Disordered Proteins. [PDF]

Methods Protoc
Senćanski M.
europepmc   +1 more source

How protein hydration depends on amino acid composition, peptide conformation, and force fields. [PDF]

Biophys J
Linse JB, Fischbach TM, Hub JS.
europepmc   +1 more source

DR and SPIT: Statistical approaches for identifying transient structure in intrinsically disordered proteins via NMR chemical shifts. [PDF]

Protein Sci
Kovács D, Bodor A.
europepmc   +1 more source

The Monomeric Conformational Ensembles of Aβ40 and Aβ42 Encode Their Differential Amyloid Aggregation Propensity. [PDF]

J Phys Chem B
Cadenelli I, Ciccolo A, Tagliabue A, Rossi G, Conti Nibali V, Bochicchio D.   +5 more
europepmc   +1 more source

An ALS-associated mutation in the C-terminal α-helix of TDP-43 uncouples condensate formation and amyloid assembly. [PDF]

Protein Sci
Byrd EJ, Crossley JA, Chau CCC, Actis P, Calabrese AN.   +4 more
europepmc   +1 more source

A study of Protean Segments (ProSs):- Short regions in Intrinsically Disordered Proteins (IDPs) that undergo disorder-to-order transitions upon binding

A study of Protean Segments (ProSs):- Short regions in Intrinsically Disordered Proteins (IDPs) that undergo disorder-to-order transitions upon binding
openaire  

IDP–CRF: Intrinsically Disordered Protein/Region Identification Based on Conditional Random Fields [PDF]

International Journal of Molecular Sciences, 2018
Accurate prediction of intrinsically disordered proteins/regions is one of the most important tasks in bioinformatics, and some computational predictors have been proposed to solve this problem. How to efficiently incorporate the sequence-order effect is
Yumeng Liu, Xiaolong Wang, Wang Xiaolong   +2 more
exaly   +4 more sources

Phanto-IDP: compact model for precise intrinsically disordered protein backbone generation and enhanced sampling

Briefings in Bioinformatics, 2023
Abstract The biological function of proteins is determined not only by their static structures but also by the dynamic properties of their conformational ensembles. Numerous high-accuracy static structure prediction tools have been recently developed based on deep learning; however, there remains a lack of efficient and accurate methods ...
Hai-Feng Chen
exaly   +3 more sources

Some of the next articles are maybe not open access.

Related searches:

A three-state mechanism for trifluoroethanol denaturation of an intrinsically disordered protein (IDP)

The Journal of Biochemistry, 2023
Abstract Relating the amino acid composition and sequence to chain folding and binding preferences of intrinsically disordered proteins (IDPs) has emerged as a huge challenge. While globular proteins have respective 3D structures that are unique to their individual functions, IDPs violate this structure–function paradigm because rather ...
Mujahid Hossain, Noorul Huda, Abani K Bhuyan   +2 more
openaire   +2 more sources