Key features determining the specificity of aspartic proteinase inhibition by the helix-forming IA3 polypeptide
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The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae
Phylip LH, Lees WE, Brownsey BG, Bur D, Dunn BM, Winther JR, Gustchina A, Li M, Copeland T, Wlodawer A Kay J (2001) The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae. J Biol Chem 276, 2023 2030.
The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix
Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J Gustchina A (2000) The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix. Nat Struct Biol 7, 113 117.
Adaptation of the behaviour of an aspartic proteinase inhibitor by relocation of a lysine residue by one helical turn
Winterburn TJ, Wyatt DM, Phylip LH, Berry C, Bur D Kay J (2006) Adaptation of the behaviour of an aspartic proteinase inhibitor by relocation of a lysine residue by one helical turn. Biol Chem 387, 1139 1142.
Characterizing the residue level folding of the intrinsically unstructured IA3
Ganesh OK, Green TB, Edison AS Hagen SJ (2006) Characterizing the residue level folding of the intrinsically unstructured IA3. Biochemistry 45, 13585 13596.
IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution
Green T, Ganesh O, Perry K, Smith L, Phylip LH, Logan TM, Hagen SJ, Dunn BM Edison AS (2004) IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution. Biochemistry 43, 4071 4081.
Desktop prediction/ analysis of mass spectrometric data in proteomic projects by using massXpert
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