Sentence examples for structure of valine from inspiring English sources

The chemical structure of valine is.

The 2.9 angstrom crystal structure of the valine tRNA-synthetase (valRS) from Thermus thermophilius [PDB id: 1IVS (Fukai et al. 2003)] was used as a template for constructing a structural model of the valRS from C. elegans (glp-4 VARS-2, see below).

The third group, branched-chain amino acids (BCAA), contains leucine and isoleucine, which have a similar structure to valine.

Beyond the changes in covalent structure caused by substitution of valine for histidine at residue 87, there is strikingly little alteration within this region of the protein.

The predicted secondary structure features an alpha helical structure, with an unusually high percentage of valine residues.

This model was constructed by replacing the side chain of the conserved glycine (G283) in the fully reduced wild-type Rs crystal structure (PDB entry 3FYE) with that of valine in the conformation found in the crystal structure of the G232V ba3 enzyme presented here.

Coordinates for the fully reduced G232V mutant were obtained from the production simulations of the wild-type enzyme after replacing the G232 side chain with that of valine in the conformation observed in the crystal structure presented here.

A caveat to this detailed structural interpretation is that in the significantly differing local geometry of monomer B in the PDB code 4LAW structure of FKBP52 the introduction of the valine residue side chain at residue 118 does not appear to yield a severe steric conflict.

Model building from the high-resolution X-ray structure of human FKBP12 [ 30] indicated an internal cavity which readily accommodates the second methyl group of valine without apparent steric conflict.

Validation of the side chain conformation of valine, leucine, and isoleucine residues using methyl C chemical shift data establishes that these solution structures represent the highest populated rotamers of these residues in solution.

The Cγ1 atom of Val lies upon the histidine Cγ atom of the wild-type structure, while the valine Cγ2 projects toward the face of the aromatic ring of Tyr which is not displaced but appears to become more constrained.