Results 191 to 200 of about 37,441 (229)

Catalytic Oligopeptide Synthesis

Organic Letters, 2018
Waste-free catalytic assembly of α-amino acids is fueled by a multiboron catalyst that features a characteristic B3NO2 heterocycle, providing a versatile catalytic protocol wherein functionalized natural α-amino acid units are accommodated and commonly used protecting groups are tolerated.
Zijian Liu   +3 more
openaire   +2 more sources

Docking of oligopeptides

Russian Chemical Bulletin, 2019
The paper presents the results concerning the use of the supercomputer docking program SOL-P, which performs a search for low-energy minima of protein—ligand complexes in the MMFF94 force field without using a grid of precalculated potentials for protein—ligand interactions. The SOL-P docking program can be applied to the generalized docking of ligands
A. V. Sulimov   +6 more
openaire   +1 more source

Electronic structure analysis of glycine oligopeptides and glycine–tryptophan oligopeptides

Physica E: Low-dimensional Systems and Nanostructures, 2014
Abstract Using the density functional theory (DFT), we have studied the energy gap, charge distribution, density of states and chemical activity of glycine (Gn) oligopeptides and glycine–tryptophan (GWn) oligopeptides. The results show that: (1) with the increasing of Gn residues, the chemical activity of Gn oligopeptides focuses on the terminal ...
Xin Li   +5 more
openaire   +1 more source

Oligopeptide cyclophilin inhibitors: A reassessment

European Journal of Medicinal Chemistry, 2011
Potent cyclophilin A (CypA) inhibitors such as non-immunosuppressive cyclosporin A (CsA) derivatives have been already used in clinical trials in patients with viral infections. CypA is a peptidyl prolyl cis/trans isomerase (PPIase) that catalyzes slow prolyl bond cis/trans interconversions of the backbone of substrate peptides and proteins.
Michael, Schumann   +4 more
openaire   +2 more sources

Thermolysin: Kinetic Study with Oligopeptides

European Journal of Biochemistry, 1970
Thermolysin is a well‐known protease which exhibits its specificity against hydrophobic amino acid residues such as l‐leucine, l‐phenylalanine, etc. whose amino groups donate the susceptible peptide bonds (amino‐endopeptidase). The present study was undertaken to investigate the effects of neighboring residues surrounding the sensitive amino acid ...
K, Morihara, H, Tsuzuki
openaire   +2 more sources

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