Results 101 to 110 of about 5,123 (214)

Many-to-one binding by intrinsically disordered protein regions

, 2019
Disordered binding regions (DBRs), which are embedded within intrinsically disordered proteins or regions (IDPs or IDRs), enable IDPs or IDRs to mediate multiple protein-protein interactions.
Andrzej Kloczkowski, A. Keith Dunker, Faraggi, Eshel, Huang, Fei, Pedro Romero, Oldfield, Christopher J., Bin Xue, Vladimir N. Uversky, Christopher J. Oldfield, Meng, Jingwei, Eshel Faraggi, Uversky, Vladimir N., Fei Huang, Dunker, A. Keith, Kloczkowski, Andrzej, Jingwei Meng, Wei-Lun Alterovitz, Alterovitz, Wei-Lun, Xue, Bin, Romero, Pedro   +19 more
core   +1 more source

Advances and challenges in multiscale biomolecular simulations: artificial intelligence‐driven paradigm shift

Quantitative Biology, Volume 14, Issue 2, June 2026.
Abstract Molecular simulation techniques have become an invaluable tool for elucidating the fundamental principles of life at the molecular level. After nearly five decades of development, biomolecular simulations have evolved to enable the quantitative characterization of complex biomolecular events, such as protein folding, conformational dynamics ...
Wenfei Li, Wei Wang
wiley   +1 more source

Electrostatics in intrinsically disordered proteins

, 2012
Protein-protein interactions are fundamental to many biological processes. A large proportion of proteins have been identified as partially or entirely disordered in their native state.
Wong, Eric Tsz Chung
core  

Effects of macromolecular crowding on an intrinsically disordered protein

, 2022
Proteins are composed of amino acids, and usually have one native structure. Intrinsically disordered proteins lack a native structure and can populate many different forms, making them ideal for binding.
Hadfield, Andrew
core  

Conformationally adaptive therapeutic peptides for diseases caused by intrinsically disordered proteins (IDPs). New paradigm for drug discovery: Target the target, not the arrow

Pharmacology & Therapeutics
The traditional model of protein structure determined by the amino acid sequence is today seriously challenged by the fact that approximately half of the human proteome is made up of proteins that do not have a stable 3D structure, either partially or in totality. These proteins, called intrinsically disordered proteins (IDPs), are involved in numerous
Jacques, Fantini, Fodil, Azzaz, Coralie, Di Scala, Anaïs, Aulas, Henri, Chahinian, Nouara, Yahi   +5 more
  +6 more sources

Protein design and RNA design: Perspectives

Quantitative Biology, Volume 14, Issue 2, June 2026.
Abstract Advances in deep learning and generative modeling have transformed the landscape of protein and RNA design, enabling rapid and precise creation of novel biomolecules with tailored structures and functions. In protein design, generative deep learning frameworks now support backbone generation, sequence optimization, and joint sequence–structure
Xi Chen, Xu Dai, Peilong Lu
wiley   +1 more source

Opportunities and challenges in protein structure prediction

Quantitative Biology, Volume 14, Issue 2, June 2026.
Abstract Deep learning methods, particularly exemplified by AlphaFold2, have revolutionized the field of protein structure prediction—an achievement recognized by the 2024 Nobel Prize in Chemistry awarded to its core developers. Despite this remarkable achievement, the broader protein folding problem is far from solved. Key challenges—each representing
Wenkai Wang, Baoquan Su, Chenxiao Xiang, Jianyi Yang   +3 more
wiley   +1 more source

On‐Chip Evaluation of Red Blood Cell Deformability Through Transit Velocity Index in Hematological Diseases

Small, Volume 22, Issue 33, 12 June 2026.
The deformability of red blood cell is essential for smooth microcirculation. We propose a deformability index using a microfluidic platform with capillary‐like constrictions, based on the relationship between cell deformation and transit velocity through the constrictions. Its effectiveness and clinical potential have been demonstrated in applications
Kenji Kajitani, Chia‐Hung Dylan Tsai, Tomohito Ohtani, Shigeo Wada, Ivan Cimrák, Misato Chimura, Tatsunori Taniguchi, Yasutaka Ueda, Jun‐ichi Nishimura, Yasushi Sakata   +9 more
wiley   +1 more source

Therapeutic Peptide SS‐31 Modulates Membrane Binding and Aggregation of α‐Synuclein and Restores Impaired Mitochondrial Function

Chemical Biology &Drug Design, Volume 107, Issue 6, June 2026.
SS‐31 (Elamipretide) inhibits α‐synuclein aggregation on the membranes and emerges as a promising therapeutic candidate against mitochondrial dysfunction in Parkinson's disease. ABSTRACT Membrane binding and aggregation properties of α‐synuclein are closely associated with Parkinson's disease and a class of related syndromes named as synucleinopathy ...
Ewelina Stefaniak, Beiyuan Cui, Xucheng Yan, Kexin Sun, Xiangyu Teng, Liming Ying   +5 more
wiley   +1 more source

Investigating Intra- and Inter-Molecular Coevolution of Intrinsically Disordered Protein, Prothymosin-alpha

, 2023
Prothymosin-a (ProTa) is a small, highly acidic protein found in the nuclei of virtually all mammalian tissues. It belongs to a class of proteins known for their lack of a rigid three-dimensional structure called intrinsically disordered proteins (IDPs).
Biscardi, Brianna, NC DOCKS at East Carolina University   +1 more
core