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.
Dwyer, John J
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] - Biochemistry May 2003 - 4945-53 p. digital
Publication Type: Journal Article
0006-2960
10.1021/bi027283n doi
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
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] - Biochemistry May 2003 - 4945-53 p. digital
Publication Type: Journal Article
0006-2960
10.1021/bi027283n doi
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