Intra-molecular Conformational Stability in Human Growth Hormone

  • R. P. Koirala Tribhuvan University, Kathmandu, Nepal
  • B. Thapa Padma Kanya Multiple Campus, Tribhuvan University, Kathmandu, Nepal
  • S. P. Khanal Tribhuvan University, Kathmandu, Nepal
  • R. P. Adhikari Kathmandu University, Dhulikhel, Nepal
  • N. P. Adhikari Tribhuvan University, Kathmandu, Nepal
Keywords: Intra-binding, growth hormone, hydrophobic, aromatic

Abstract

Human growth hormone (hGH) is synthesized, stored and secreted by somatotropic cells within the lateral wings of the anterior lobe of pituitary glands; and is transported to other organs of human body. Study of intra-molecular structure and its binding mechanisms within the molecule gives more insight of structural stability of the molecule and is also essential in drug designing. In this article, we have investigated the various bonded and non-bonded interactions that contribute for the conformation of entire structure of the hGH molecule using molecular dynamics (MD) simulation. The MD outcomes show that the molecule is hydrophobic in nature. In its conformation, several types of interactions exist, such as disulphide bridges (bonded) and nonbonded: hydrogen bond, hydrophobic, aromatic-aromatic, ionic, aromatic-sulphur, cation-pi.

Downloads

Download data is not yet available.
Abstract
88
pdf
73

Author Biographies

R. P. Koirala, Tribhuvan University, Kathmandu, Nepal

Central Department of Physics

S. P. Khanal, Tribhuvan University, Kathmandu, Nepal

Central Department of Physics

R. P. Adhikari, Kathmandu University, Dhulikhel, Nepal

Department of Natural Sciences

N. P. Adhikari, Tribhuvan University, Kathmandu, Nepal

Central Department of Physics

Published
2020-12-31
How to Cite
Koirala, R., Thapa, B., Khanal, S., Adhikari, R., & Adhikari, N. (2020). Intra-molecular Conformational Stability in Human Growth Hormone. Journal of Nepal Physical Society, 6(2), 41-49. https://doi.org/10.3126/jnphyssoc.v6i2.34856
Section
Articles