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Exploration of Conformations, Analysis of Protein and Biological Significance of Histidine Dimers
Author(s) -
Uppula Purushotham
Publication year - 2018
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.201702559
Subject(s) - protein data bank (rcsb pdb) , histidine , protein data bank , hydrogen bond , conformational isomerism , chemistry , covalent bond , crystallography , non covalent interactions , density functional theory , computational chemistry , protein structure , stereochemistry , molecule , amino acid , biochemistry , organic chemistry
The exhaustive conformational search of histidine dimers (HisD) carried out using density functional theory (DFT). A large number of non‐covalent interactions and hydrogen bonding interactions stabilized various forms of HisDs that resulted 143 unique conformers. The HisDs which have hydrogen bonding interactions are more stable than other HisDs with aromatic‐aromatic interactions. In addition, search of HisDs in proteins that deposited in the protein data bank shows a significant increase of HisDs appear from 4 Å to 6 Å centroid‐centroid distance. Further, the angle analysis between two π planes resulted that the number of dimers is more abundant at 31°‐ 60° angles which shows that HisD prefers tilted and parallel displaced orientations in the proteins. The above observations from protein data bank (PDB) analysis show good agreement with DFT calculations of the histidine dimers. In conclusion, the subtle balance between non‐covalent interactions determine the conformational preferences of histidine dimers.