Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns

Science

Volumn 331, Issue 6017, 2011, Pages 571-575

  Culyba, Elizabeth K ^a   Price, Joshua L ^a   Hanson, Sarah R ^a   Dhar, Apratim ^b   Wong, Chi Huey ^a   Gruebele, Martin ^b   Powers, Evan T ^a   Kelly, Jeffery W ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; GLYCAN; GLYCOPROTEIN; N ACETYLGLUCOSAMINE; PHENYLALANINE;

GENETIC ANALYSIS; PROTEIN; SECRETION; STABILIZATION;

ARTICLE; ELECTROSPRAY; PRIORITY JOURNAL; PROTEIN DATA BANK; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN GLYCOSYLATION; PROTEIN INTERACTION; PROTEIN STABILITY; SECRETORY PATHWAY; THERMODYNAMICS; WESTERN BLOTTING;

ACETYLGLUCOSAMINE; ACID ANHYDRIDE HYDROLASES; AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, CD2; ASPARAGINE; GLYCOSYLATION; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PEPTIDYLPROLYL ISOMERASE; PHENYLALANINE; POLYSACCHARIDES; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; RATS; THERMODYNAMICS;

EUKARYOTA;

EID: 79551626904     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1198461     Document Type: Article

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31. We thank R. A. Dwek, I. A. Wilson, J. C. Paulson, S. Deechongkit, and D. L. Powers for presubmission reviews and for helpful prepublication discussions. This work was supported in part by the Skaggs Institute for Chemical Biology, the Lita Annenberg Hazen Foundation, and by NIH grant GM051105 to J.W.K. and E.T.P. J.L.P. was supported in part by NIH postdoctoral fellowship F32 GM086039. A.D. and M.G. were supported by NSF grant MCB 1019958. S.R.H. and C.-H.W. were supported by NIH grant AI072155. The Scripps Research Institute has filed a provisional patent application covering the results described in this paper.