Results 31 to 40 of about 357,415 (263)
Characterization of Trypsin-Like Protease of Lactobacillus plantarum FNCC 0270
Trypsin is an enzyme that has a unique mechanism of cutting peptide bonds specifically at the carboxyl side of lysine or arginine amino acids, with another amino acid.
Trismilah Margono +3 more
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Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation
Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang +2 more
wiley +1 more source
The prediction of polypeptide chain fragmentation during digestion (proteolysis) of protein substrates by trypsin was carried out for globular β-lactoglobulin (β-LG) and micellar β-casein (β-CN).
Mikhail M. Vorob’ev
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Predicting peptide structures in native proteins from physical simulations of fragments. [PDF]
It has long been proposed that much of the information encoding how a protein folds is contained locally in the peptide chain. Here we present a large-scale simulation study designed to examine the extent to which conformations of peptide fragments in ...
Vincent A Voelz +2 more
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Translophagy—A potential link between autophagy impairment and translational errors
Neurodegenerative diseases are characterised by the accumulation of abnormal proteins and protein aggregates, but their origin often remains unknown. We propose that selective autophagy removes damaged protein‐making machinery, preventing errors during protein synthesis.
Mykola V. Korolchuk +11 more
wiley +1 more source
Pfs230 is a leading malaria transmission blocking vaccine (TBV) candidate. Comprising 3135 amino acids (aa), the large size of Pfs230 necessitates the use of sub-fragments as vaccine immunogens. Therefore, determination of which regions induce functional
Kazutoyo Miura +13 more
doaj +1 more source
Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav +2 more
wiley +1 more source
The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation
Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge +6 more
wiley +1 more source
Kelly Limi Aida,1 Paula Fernanda Kreling,1 Karina Sampaio Caiaffa,2 Giovana Maria Fioramonti Calixto,3 Marlus Chorilli,3 Denise MP Spolidorio,4 Norival Alves Santos-Filho,5,6 Eduardo Maffud Cilli,5 Cristiane Duque1 1Department of Pediatric Dentistry and
Aida KL +8 more
doaj
Mass spectrometry is a leading method used for sequencing peptides and proteins by fragmentation followed by analysis of the sequence fragments. Here, the authors use infrared spectroscopy to characterize the structures of peptide fragments formed during
Jonathan Martens +3 more
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