Insights into the mechanism and catalysis of the native chemical ligation reaction

Journal of the American Chemical Society

Volumn 128, Issue 20, 2006, Pages 6640-6646

  Johnson, Erik C B ^a,b   Kent, Stephen B H ^a,b  

^a UNIVERSITY OF CHICAGO   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHEMICAL REACTIONS; ESTERS; REACTION KINETICS; SYNTHESIS (CHEMICAL);

CHEMICAL LIGATION; CYSTEINE-PEPTIDES; THIOALKYL ESTERS; TRANSTHIOESTERIFICATION;

PROTEINS;

CYSTEINE; MESNA; PEPTIDE; THIOL;

ANALYTIC METHOD; ARTICLE; CATALYSIS; CHEMICAL REACTION; COVALENT BOND; ESTERIFICATION; MOLECULAR BIOLOGY; MOLECULAR INTERACTION; PKA; PROTEIN SYNTHESIS; REACTION ANALYSIS;

CATALYSIS; CYSTEINE; ESTERS; HYDROGEN-ION CONCENTRATION; OVOMUCIN; PEPTIDES; PHENYLACETATES; PROTEINS; SULFHYDRYL COMPOUNDS;

EID: 33646728877     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja058344i     Document Type: Article

References (15)

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13. Thiophenol is only sparingly soluble in water: in solubility tables it is listed as insoluble in water. It behaves as if soluble only to ∼20 mM (based on ∼ 10-fold rate difference between thiophenol and MPAA, in Table 2). The data in Figure 4 also support this-the ligation rate in the presence of 1% thiophenol (nominally ∼90 mM. but visibly not completely dissolved) is what would be expected for ∼20 mM MPAA.
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