Insertion of a synthetic peptide into a recombinant protein framework: A protein biosensor [7]

Journal of the American Chemical Society

Volumn 121, Issue 5, 1999, Pages 1100-1101

  Cotton, Graham J ^a   Ayers, Brenda ^a   Xu, Rong ^a   Muir, Tom W ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

RECOMBINANT PROTEIN; SYNTHETIC PEPTIDE;

BIOSYNTHESIS; GENETIC ENGINEERING; GENETIC RECOMBINATION; LETTER; PEPTIDE SYNTHESIS; PROTEIN EXPRESSION; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;

EID: 0033540665     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja983804b     Document Type: Letter

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33. 6 according to the in situ neutralization protocols for Boc solid-phase peptide synthesis: Schnölzer, M.; Alewood, P.; Jones, A.; Alewood, D.; Kent, S. B. H. Int. J. Pept. Protein Res. 1992, 40, 180-193. The Dns group was incorporated directly as the α-(t-Boc)-ε-(4-dimethylaminonaphthalene-1-sulfonyl) derivative of lysine.
34. 121)SH2 was generated by factor Xa treatment of a precursor GST fusion protein containing the sequence IIe-Glu-Gly-Arg-Cys immediately N-terminal to the SH2 domain (see refs 1k and 8).
35. 120 was mutated to Gly to improve the kinetics of the ligation reaction (see ref 1k).
36. α-protecting group was 28%.
37. The protein was refolded by rapid dilution (>10-fold) from 6 M GdmCl with 10 mM DTT, 140 mM NaCl, 25 mM phosphate pH 7.2.
38. 6]-lysine; 3BP2 is PPAYPPPPVP; 2BP1 is PVY*ENV (Y* = phosphotyrosine).
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40. Structural studies on fully recombinant Abl-SH(32) indicate that the relative orientation of the SH2 and SH3 domains is not restricted in solution (ref 4b).