Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120.

Lignende værker

• Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin.
  af: Sano, T, et al.
  Udgivet: (1995)
• Studies on the biotin-binding site of streptavidin. Tryptophan residues involved in the active site.
  af: Gitlin, G, et al.
  Udgivet: (1988)
• Streptavidin and its biotin complex at atomic resolution
  af: Le Trong, Isolde, et al.
  Udgivet: (2011)
• Second Contact Shell Mutation Diminishes Streptavidin-Biotin Binding Affinity Through Transmitted Effects on Equilibrium Dynamics
  af: Baugh, Loren, et al.
  Udgivet: (2012)
• A Streptavidin Binding Site Mutation Yields an Unexpected Result: An Ionized Asp128 Residue is Not Essential for Strong Biotin Binding
  af: Baugh, Loren, et al.
  Udgivet: (2016)