Abstract
Background:HIV-1 infectivity is decreased by specific mutations that alter the hydrophobicity level in the HIV-1 gp41 loop core. Results:Antibody recognition, disulfide-bond formation, and lipid mixing of loop domain peptides are strongly affected by these mutations. Conclusion:The hydrophobic core maintains proper function and structure of the loop region. Significance:A better understanding of the membrane fusion mechanism of HIV and similar viruses is provided.
| Original language | English |
|---|---|
| Pages (from-to) | 29143-29150 |
| Number of pages | 8 |
| Journal | Journal of Biological Chemistry |
| Volume | 288 |
| Issue number | 40 |
| DOIs | |
| State | Published - 4 Oct 2013 |
| Externally published | Yes |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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