Results 131 to 140 of about 23,829 (240)
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 +5 more
+6 more sources
Protein design and RNA design: Perspectives
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
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 +3 more
wiley +1 more source
A proline switch explains kinetic heterogeneity in a coupled folding and binding reaction
How intrinsically disordered proteins (IDPs) undergo a coupled folding and binding reaction with their molecular targets remains to be understood. Here authors use single-molecule FRET to assess the contribution of cis/trans isomerization of peptidyl ...
Franziska Zosel +3 more
doaj +1 more source
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 +9 more
wiley +1 more source
Abstract Identification of intrinsically disordered regions (IDRs) in proteins is essential for understanding fundamental cellular processes. The IDRs can be divided into long disordered regions (LDRs) and short disordered regions (SDRs) according to their lengths.
Junxi Xie +4 more
openaire +2 more sources
Denaturant-Induced Conformational Transitions in Intrinsically Disordered Proteins
Intrinsically disordered proteins (IDPs) differ from ordered proteins at several levels: structural, functional, and conformational. Amino acid biases also drive atypical responses of IDPs to changes in their environ- ment.
Ciurli, Stefano +7 more
core +1 more source
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 +5 more
wiley +1 more source
Diffusion-limited association of disordered protein by non-native electrostatic interactions
Intrinsically disordered proteins (IDPs) usually fold during binding to target proteins which involves the formation of a transient complex (TC). Here authors use single-molecule FRET to show that the lifetime of TC for IDP binding is very long due to ...
Jae-Yeol Kim +3 more
doaj +1 more source
Recent Advances in Computational Protocols Addressing Intrinsically Disordered Proteins
Intrinsically disordered proteins (IDP) are abundant in the human genome and have recently emerged as major therapeutic targets for various diseases. Unlike traditional proteins that adopt a definitive structure, IDPs in free solution are disordered and ...
Supriyo Bhattacharya, Xingcheng Lin
doaj +1 more source

