Results 51 to 60 of about 2,005,992 (360)
The synthesis of difficult peptide sequences has been a challenge since the very beginning of SPPS. The self‐assembly of the growing peptide chains has been proposed as one of the causes of this synthetic problem.
Dolors Grillo-Bosch+2 more
semanticscholar +1 more source
Mapping of residues of fibrinogen cleaved by protease II of Bacillus thuringiensis var. israelensis IMV B-7465 [PDF]
The limited proteolysis of macromolecules allows obtaining the fragments that preserve the structure and functional properties of the whole molecule and could be used in the study of proteins structure and function.
E. M. Stohniy+8 more
doaj +1 more source
Modeling of protein-peptide interactions using the CABS-dock web server for binding site search and flexible docking [PDF]
Protein-peptide interactions play essential functional roles in living organisms and their structural characterization is a hot subject of current experimental and theoretical research. Computational modeling of the structure of protein-peptide interactions is usually divided into two stages: prediction of the binding site at a protein receptor surface,
arxiv +1 more source
Peptide splicing is a newly described mode of production of antigenic peptides presented by MHC class I molecules, whereby two noncontiguous fragments of the parental protein are joined together after excision of the intervening segment.
Alexandre Dalet+4 more
semanticscholar +1 more source
Insertion of the FeB cofactor in cNORs lacking metal inserting chaperones
Nitric oxide reductase is an enzyme found in the bacterial denitrification pathway. The NOR active site contains a non‐heme iron, often, but not always inserted with the assistance of chaperones. Here, we study the insertion of FeB in the subfamily of cNORs lacking chaperones and found a putative channel, conserved in the family, perhaps enabling the ...
Sofia Appelgren, Pia Ädelroth
wiley +1 more source
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
doaj +1 more source
Immunomodulatory and neurotropic activities of synthetic peptides in a model of brain injury in rats
Treatment of consequences of traumatic brain injury (TBI) remains one of the current problems of medicine. To increase the effectiveness of treatment of post-traumatic complications, various drugs are recommended, including the peptide with ...
N. B. Serebryanaya+5 more
doaj +1 more source
Background Celiac disease is a T-cell mediated chronic inflammatory disorder of the gut that is induced by dietary exposure to gluten proteins. CD4+ T cells of the intestinal lesion recognize gluten peptides in the context of HLA-DQ2.5 or HLA-DQ8 and the
Siri Dørum+7 more
semanticscholar +1 more source
LHCPs are transported to the thylakoid membrane via the (cp)SRP pathway. This process involves a transit complex of (cp)SRP43, (cp)SRP54 and LHCP, which interacts with (cp)FtsY and Alb3 at the membrane. GTP hydrolysis by (cp)SRP54 and (cp)FtsY triggers complex dissociation.
Victor Zegarra+7 more
wiley +1 more source
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
doaj +1 more source