The hydrophobic pocket contributes to the structural stability of the N-terminal coiled coil of HIV gp41 but is not required for six-helix bundle formation. [electronic resource]
Producer: 20030625Description: 4945-53 p. digitalISSN:- 0006-2960
- Amino Acid Sequence
- Binding Sites
- Circular Dichroism
- Drug Stability
- HIV -- physiology
- HIV Envelope Protein gp41 -- chemistry
- Membrane Fusion
- Molecular Sequence Data
- Molecular Weight
- Peptide Fragments -- chemistry
- Protein Structure, Secondary
- Sequence Alignment
- Sequence Homology, Amino Acid
- Software
- Thermodynamics
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Publication Type: Journal Article
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