Results 121 to 130 of about 23,829 (240)
Abstract The pathological expansion of the polyglutamine (polyQ) repeat within the first exon of huntingtin (Httex1) protein is a defining hallmark of Huntington's disease (HD). Multiple evidence supports that the membrane recruitment of Httex1 is critical for its self‐assembly and related toxicity in HD.
Tânia Sousa +6 more
wiley +1 more source
Unusual Biophysics of Intrinsically Disordered Proteins
Research of a past decade and a half leaves no doubt that complete understanding of protein functionality requires close consideration of the fact that many functional proteins do not have well-folded structures.
Uversky, Vladimir N.
core +1 more source
Dynamic disorder is crucial for mitochondrial protein import
Abstract The import of proteins into mitochondria poses fundamental mechanistic challenges: aggregation‐prone precursor proteins must be maintained in aqueous compartments and threaded through narrow pores without becoming stuck or mislocalized. Recent evidence from mitochondrial protein import studies and other chaperone systems underscores the ...
Jakob Schneider +3 more
wiley +1 more source
Structural analysis of intrinsically disordered proteins: computer atomistic simulation [PDF]
Intrinsically disordered proteins (IDPs) are biomolecules that do not have a definite 3D structure; their role in the biochemical network of a cell relates to their ability to switch rapidly among different secondary and tertiary structures.
Ciasca, Gabriele +2 more
core
Sketching microprotein portraits
Abstract The illustrations of intricate molecular machineries inside cells created by David Goodsell continue to inspire the scientific community. Here, we aim to extend his artworks to include microproteins, a newly recognized class of small proteins with less than 100 amino acids, encoded by small open reading frames.
Gabriel Diaz +6 more
wiley +1 more source
Structural disorder of plasmid-encoded proteins in Bacteria and Archaea
Background In the last decade and a half it has been firmly established that a large number of proteins do not adopt a well-defined (ordered) structure under physiological conditions.
Nenad S. Mitić +4 more
doaj +1 more source
Use of biomolecular emulator for characterizing flexible proteins by small‐angle x‐ray scattering
Abstract Flexible proteins populate heterogeneous conformational ensembles that are essential for their function. Small‐angle x‐ray scattering (SAXS) is widely used to study protein structure in solution and to characterize conformational heterogeneity.
Yoni Haitin, Bar Manori, Moshe Giladi
wiley +1 more source
Long-Range Correlated Dynamics in Intrinsically Disordered Proteins
*S Supporting Information ABSTRACT: Intrinsically disordered proteins (IDPs) are involved in a wide variety of physiological and pathological processes and are best described by ensembles of rapidly interconverting conformers.
Stefan Becker +17 more
core +1 more source
Intrinsically Disordered Proteins & Regions in Viruses and Possibly Pharmaceuticals
This review examines the significance of intrinsically disordered proteins (IDPs) and regions to viruses and their prospects as vaccine components. Using a content analysis of scientific articles, reviews, interviews, industry updates and magazines, it ...
Cerda, Nicholas Alexander
core +1 more source
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

