Sentence examples for structure of proline from inspiring English sources

The chemical structure of proline is.

Due to the unique structure of proline and the formation of disulfate bonds by cysteine, these residues have considerable impacts on the protein structures.

It is possible that the ring structure of proline might allow the substrate to be recognised in a different orientation within the PAT2 binding site or even in distinct orientations (as both an α- and a δ-imino acid) which might help explain why both d-proline and trans-4-hydroxy l-proline have similar affinities for PAT2 to that observed with l-proline [26,27,37,38].

The distinctive cyclic structure of proline's side chain gives it an exceptional conformational rigidity, interfering in peptide bond formation with other amino acids and affecting the secondary structure of the protein [ 27].

The novel S59P mutation determines the presence in the TNF-R1 of one more proline residue, which might interfere with three-dimensional receptor folding, since the distinctive cyclic structure of proline's side chain gives it an exceptional conformational rigidity and might cause a bend in the receptor's secondary amino acid structure [ 27].

Comparison of protein 3D structures of proline peptidases PepI/PepR/PepL and esterase A allowed identification of a conserved core structure, which was then used to improve phylogenetic analysis and functional annotation within this protein superfamily.

The results herein in α-helices stand in contrast to the results of our previous investigation of the effects of phosphorylation and OGlcNAcylation on the structure of the proline-rich domain of tau and of proline-rich model peptides.

The spatial structure of the proline-rich domain is still unsolved.

The conservation of sequence and genomic structure of this Proline-rich linker throughout metazoan evolution (see Additional files 2 and 3) supports a key role in positioning H1 and H2 relative to each other and contribution to the DNA-binding specificity of COE dimers.

In the final structure of saquinavir, the proline was replaced by a z(S,S,S -decahydro-isoquinoline- 3-carbonyl (DIQ) group to enhance the inhibitory potency.

We previously observed that phosphothreonine is a particularly conformationally restricted amino acid, capable of adopting a structure similar to that of proline via two noncovalent interactions: (1) side chain cyclization via side chain main chain phosphate amide hydrogen bonding and (2) an n → π* interaction between consecutive carbonyls.