Electrostatic energy calculation on the pH-induced conformational change of influenza virus hemagglutinin

Sup Choi Ho, June Huh, Ho Jo Won

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The pH-induced conformational change of influenza virus hemagglutinin (HA) has been investigated by calculating the change of electrostatic energy of the fragment of HA2 upon pH change. The average charge and electrostatic free energy are calculated as a function of pH for the fusion peptide (residues 1-20 of HA2) and the polypeptide of residues 54-77 of HA2 by using the finite difference Poisson-Boltzmann method. It is found that as pH decreases from 8 to 5, the electrostatic free energy of the fusogenic state is lowered by ∼2 kcal/mol and the fusogenic state is less ionized compared to that of the native state for both polypeptides. For the fusion peptide at the fusogenic state, most of ionizable residues are neutral at acidic pH except Glu-11. For the polypeptide of residues 54-77 at the fusogenic state, most of residues except Glu-74 and His-64 are fully charged between pH 5 and pH 8.

Original languageEnglish
Pages (from-to)55-60
Number of pages6
JournalBiophysical Journal
Volume91
Issue number1
DOIs
Publication statusPublished - 2006 Jan 1
Externally publishedYes

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Hemagglutinins
Orthomyxoviridae
Static Electricity
Peptides

ASJC Scopus subject areas

  • Biophysics

Cite this

Electrostatic energy calculation on the pH-induced conformational change of influenza virus hemagglutinin. / Ho, Sup Choi; Huh, June; Won, Ho Jo.

In: Biophysical Journal, Vol. 91, No. 1, 01.01.2006, p. 55-60.

Research output: Contribution to journalArticle

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