Sentence examples for maintaining protein structures from inspiring English sources

The key roles of these stabilizing interactions in maintaining protein structures have been previously demonstrated in a few cases, for example in the tyrosine corner [ 31], but we have shown here that there are many others important for maintaining protein stability.

The results of transgenic modifications of biosynthetic and metabolic pathways in most of the previously mentioned cases indicate that higher stress tolerance and the accumulation of compatible solutes may also protect plants against damage by scavenging of reactive oxygen species (ROS) and by their chaperone-like activities in maintaining protein structures and functions [ 64].

Disulfide bond formation between cysteine (Cys) pairs is one of the most common modifications found in extracellularly-destined proteins, key to maintaining protein structure.

The average values for all these features were used to reflect the physicochemical properties of surrounding residues and their importance in maintaining protein structure.

Conservation of buried polar residues and the hydrogen-bond interactions that they form implies an important role for maintaining protein structure, contributing strong restraints on amino acid substitutions during divergent protein evolution.

Conservation of these residues and the interactions that they form implies that they are important for maintaining protein structure and hence provide restraints on amino acid substitutions during divergent evolution.

The decreased content of cysteine (C) in disordered regions supports the lack of formation of hydrophobic cores of globular proteins because this amino acid frequently occurs in sites of activating or stabilizing disulfide bridges important for maintaining protein structure in proteins and are thus not necessary in IDPs [ 25].

Relaxed selective constraint could also result in elevated dN/dS, although there is no reason to expect that the candidate ligand genes should be under any less selective constraint than the control set of genes to maintain protein structure and function.

In order to maintain protein structure and function, a reducing intracellular environment is essential.

Nearly all enzyme activity is reduced severely at NaCl concentrations above 0.3 M because of disruption of the electrostatic forces that maintain protein structure [ 4].

Under this model, some of the amino acid substitutions in Frq1 ought to have been selected to maintain protein structure or function rather than be adaptive [ 28].