Histidine placement in de novo-designed heme proteins
作者： Brian R. Gibney , P. Leslie Dutton
DOI: 10.1110/PS.8.9.1888
关键词:
摘要: The effects of histidine residue placement in a de novo-designed four-a-helix bundle are investigated by residues at coiled coil heptad positions two distinct heptads and each position within single repeat our prototype heme protein maquette, @H10H24# 2 @$Ac-CGGGELWKL{HEELLKK{FEELLKL{HEERLKK{LCONH2%2# composed generic ~a-SS-a!2 peptide architecture. to stoichiometry variants with either or both histidines on helix replaced noncoordinating alanine ~@H10A24# 2, @A10H24# @A10A24# 2! demonstrates the obligate requirement for biologically significant affinity. Variants @$Ac-CGGGELWKL{AEELLKK{FEELLKL{AEERLKK{L-CONH2%2# containing per 9 15 were evaluated verify design based molecular modeling. bis-histidine site formed between 10 109 bound ferric hemes highest affinity, Kd1 Kd2 values 800 nM, respectively. Placement 11 ~heptad b! resulted that moderate 9.5 mM, whereas other peptides had no measurable apparent affinity .200 mM. ligation @H10A24# @H11A24# was confirmed electron paramagnetic resonance spectroscopy. rules derived from this study, together narrow tolerances revealed, applicable improving future designs, analyzing results randomized combinatorial libraries, as well implementation automated design.
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