Results 81 to 90 of about 2,589,108 (245)
Pathways and pitfalls: a qualitative study of student experiences in biomedical science education
Biomedical science students from underrepresented backgrounds face barriers including financial strain, disrupted laboratory access and cultural exclusion. Peer networks provide vital support when institutional systems are difficult to navigate. To create inclusive learning environments and achieve academic success, educators should blend active, hands‐
Olivia J. Russell +8 more
wiley +1 more source
Motivation: Protein intrinsic disorder describes the tendency of sequence residues to not fold into a rigid three-dimensional shape by themselves. However, some of these disordered regions can transition from disorder to order when interacting with ...
Zhou, Yaoqi +3 more
core +1 more source
Adenosine triphosphate as a modulator of protein interactions and stability
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley +1 more source
Unequivocal single-molecule force spectroscopy of intrinsically disordered proteins [PDF]
Intrinsically disordered proteins (IDPs) are predicted to represent about one third of the eukaryotic proteome. The dynamic ensemble of conformations of this steadily growing class of proteins has remained hardly accessible for bulk biophysical ...
Rubén Hervás +8 more
core +1 more source
We describe detailed protocols for the purification and preparation of Marchantia polymorpha Auxin Response Factor 2 (MpARF2). This protein is fused to an MBP solubility tag and an mNG fluorescent tag and is purified from Escherichia coli. The presented procedures make it possible to study MpARF2 assemblies, which could arise from phase separation ...
Bas Janssen +5 more
wiley +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
Heterotropic regulation and negative homotropic cooperativity
We identified a structural module common to some proteins that couple negative cooperativity with heterotropic regulation, two features that rarely coexist. These proteins are ring‐like and present an ordered asymmetry whereby noncontacting subunits are symmetric, and their tertiary structure differs from that of contacting subunits.
Veronica Morea +5 more
wiley +1 more source
Self-organization of intrinsically disordered proteins with folded N-termini [PDF]
Thousands of human proteins lack recognizable tertiary structure in most of their chains. Here we hypothesize that some use their structured N-terminal domains (SNTDs) to organise the remaining protein chain via intramolecular interactions, generating ...
Philip C. Simister +4 more
core
Cell surface CD11c as a neutrophil aging marker molecule
Cell surface CD11chi neutrophils were more aged and had better phagocytic function than CD11c−/lo neutrophils. Transcriptomic analysis of CD11chi neutrophils and CD11c−/lo neutrophils in pediatric population showed that the most difference was seen in infants.
Sophia Koutsogiannaki +5 more
wiley +1 more source
The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav +4 more
wiley +1 more source

