Results 71 to 80 of about 4,746 (287)
Why do eukaryotic proteins contain more intrinsically disordered regions?
Intrinsic disorder is more abundant in eukaryotic than prokaryotic proteins. Methods predicting intrinsic disorder are based on the amino acid sequence of a protein. Therefore, there must exist an underlying difference in the sequences between eukaryotic
Walter Basile +3 more
doaj +1 more source
The SARS-CoV-2 nucleocapsid (N) protein binds the viral RNA genome and contains two ordered domains flanked by three intrinsically-disordered regions. Here, the authors show that RNA binding induces liquid-liquid phase separation of N, which is driven by
Shan Lu +8 more
doaj +1 more source
The intrinsically disordered regions of eukaryotic proteomes are enriched in short linear motifs (SLiMs), which are of crucial relevance for cellular signaling and protein regulation; many mediate interactions by providing binding sites for peptide ...
Yadav, V.
core +1 more source
The potential of intrinsically disordered regions in vaccine development [PDF]
Mehrdad Ameri +2 more
openaire +2 more sources
Screening and epitope characterization of Nidogen‐2‐specific nanobodies
Camel immunization and phage display were employed to generate high‐affinity VHH nanobodies against Nidogen‐2. After library construction, biopanning, ELISA screening, sequencing, and recombinant expression, selected nanobodies were purified and characterized, leading to the preliminary exploration of a nanobody‐based sandwich ELISA for specific ...
Jianchuan Wen +9 more
wiley +1 more source
Long-Range Entropic Effects on Protein Intrinsically Disordered Regions
Entropy calculations represent one of the most challenging steps in obtaining the binding free energy in proteins and their complexes, which is a grand challenge in computational biology.
Agnieszka K., Bronowska +3 more
core +1 more source
Protein structure is determined by the amino acid sequence and a variety of post-translational modifications, and provides the basis for physiological properties.
Akshatha Ganne +7 more
doaj +1 more source
Intrinsically Disordered Proteins: An Overview
Many proteins and protein segments cannot attain a single stable three-dimensional structure under physiological conditions; instead, they adopt multiple interconverting conformational states.
Trivedi, Rakesh +1 more
core +1 more source
This study explores the feasibility of expressing the antitumoral protein Amblyomin‐X through a suicide gene therapy approach and investigates its intracellular fate after gene delivery. Although the gene is efficiently expressed, melanoma cells rapidly degrade the Amblyomin‐X protein via proteasome activity.
Victor Dal Posolo Cinel +4 more
wiley +1 more source
Expose flexible conformations for intrinsically disordered protein
The folding conformation of native protein has flexibility in different degrees, which may bring difficulty in presenting the structures, and also it causes complexity in understanding the relationship between structure and functions.
Jiaan Yang +8 more
doaj +1 more source

