Identification of structural stability of mutated Hepatitis B Virus capsid proteins by nanoenvironmental energetics measurements
by Harish Chandra Soundararajan, Muthukumaran Sivanandham
International Journal of Functional Informatics and Personalised Medicine (IJFIPM), Vol. 1, No. 3, 2008

Abstract: Hepatitis B Virus (HBV) is a commonly occurring human pathogen with an estimated 300 million carriers worldwide. This work presents a bioinformatics approach toward identifying amino acids for point mutation in Hepatitis B capsid (HBc) protein to prevent interaction of the virion's core protein with its surface protein. Based on the nanoenvironmental energetic measurements using bioinformatics tools, point mutations in the dimeric region of core protein were studied for changes in the dimensions of the key geometric parameters. The results provide structural insight regarding the important parameters contributing to HBV synthesis. This work paves the way for future pharmaceutical applications aimed at destabilisation of the HBV capsid-surface protein interactions.

Online publication date: Sat, 22-Nov-2008

The full text of this article is only available to individual subscribers or to users at subscribing institutions.

 
Existing subscribers:
Go to Inderscience Online Journals to access the Full Text of this article.

Pay per view:
If you are not a subscriber and you just want to read the full contents of this article, buy online access here.

Complimentary Subscribers, Editors or Members of the Editorial Board of the International Journal of Functional Informatics and Personalised Medicine (IJFIPM):
Login with your Inderscience username and password:

    Username:        Password:         

Forgotten your password?


Want to subscribe?
A subscription gives you complete access to all articles in the current issue, as well as to all articles in the previous three years (where applicable). See our Orders page to subscribe.

If you still need assistance, please email subs@inderscience.com