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Fig. 3 | Retrovirology

Fig. 3

From: Mutations of Glu560 within HIV-1 Envelope Glycoprotein N-terminal heptad repeat region contribute to resistance to peptide inhibitors of virus entry

Fig. 3

Biophysical characterizations of six-helix bundle (6HB) formed by N36 with indicated mutations and C34. The α-helical content is calculated from the circular dichroism (CD) spectroscopy signal at the indicated wavelengths. Unfolding is recorded at 222 nm by CD spectroscopy at the indicated temperatures, with calculated transition midpoints (Tm values) shown. The CD scanning of the complexes formed by N36 with indicated mutations and the C34 peptide (a) and their melting curves (b) are shown. c The 6HB formed by N36 with indicated mutations and C34 are visualized using native PAGE electrophoresis. The upward migration of the bands represents 6HB and lower bands represent C34 peptide. The bands of 6HB formed by C34 and N36 E560K or E560G migrated upward due to reduced negative charges of 6HB. Three panels are from the same gel, but lanes with irrelevant peptides are removed

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