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Your search keyword '"Pepermans, Henri A.M."' showing total 12 results
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12 results on '"Pepermans, Henri A.M."'

3. NMR studies of Fusarium solani pisi cutinase in complex with phosphonate inhibitors

Author

Prompers, Jeanine J., Noorloos, Brigitte van, Mannesse, Maurice L.M., Groenewegen, Anneke, Egmond, Maarten R., Verheij, Hubertus M., Hilbers, Cornelis W., and Pepermans, Henri A.M.

Subjects
Fusarium -- Research, Phosphonates -- Research, Enzyme inhibitors -- Research, Ligand binding (Biochemistry) -- Research, Rearrangements (Chemistry) -- Research, Biological sciences, Chemistry
Abstract

Research was conducted to examine the Fusarium solani cutinase in complex with phosphonate inhibitors using several nuclear magnetic resonance approaches to investigate internal motions on various time scales. A comparison of results with those of dynamical studies was carried out on free cutinase. Findings indicate that cutinase does need conformational rearrangements to bind its substrate which may develop the rate-limiting step in catalysis.

Published
1999

4. Backbone dynamics of Fusarium solani pisi cutinase probed by nuclear magnetic resonance: the lack of interfacial activation revisited

Author

Prompers, Jeanine J., Groenewegen, Anneke, Hilbers, Cornelis W., and Pepermans, Henri A.M.

Subjects
Fusarium -- Research, Nuclear magnetic resonance -- Usage, Enzyme kinetics -- Research, Enzymes -- Research, Protein binding -- Research, Biological sciences, Chemistry
Abstract

The backbone dynamics of Fusarium solani pisi cutinase are investigated using the nuclear magnetic resonance technique. An analysis of the internal motions on various time scales shows that the core of cutinase seems to exhibit high rigidity while the binding site is mobile on the microsecond to millisecond time scale. The opening and closing motions appear on a time scale which corresponds with the kinetics of the hydrolysis reaction, indicating that the conformational patterns form the rate-limiting step during catalysis.

Published
1999

10. 1H NMR study of the interaction of N, N′, N″-triacetyl chitotriose with Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus

Author

Verheyden, Patricia, Pletinckx, Jurgen, Maes, Dominique, Pepermans, Henri A.M., Wyns, Lode, Willem, Rudolph, and Martins, JoséC.

Abstract

The interaction between Ac-AMP2, a lectin-like small protein with antimicrobial and antifungal activity isolated from Amaranthus caudatus, and N, N′, N″-triacetyl chitotriose was studied using 1H NMR spectroscopy. Changes in chemical shift and line width upon increasing concentration of N, N′, N″-triacetyl chitotrioseto Ac-AMP2 solutions at pH 6.9 and 2.4 were used to determine the interaction site and the association constant Ka. The most pronounced shifts occur mainly in the C-terminal half of the sequence. They involve the aromatic residues Phe 18, Tyr 20and Tyr 27together with their surrounding residues, as well as the N-terminal Val-Gly-Glu segment. Several NOEs between Ac-AMP2 and the N, N′, N″-triacetyl chitotriose resonances are reported.

Published
1995
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11. 1H NMR study of the interaction of N,N′,N″‐triacetyl chitotriose with Ac‐AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus

Author

Verheyden, Patricia, Pletinckx, Jurgen, Maes, Dominique, Pepermans, Henri A.M., Wyns, Lode, Willem, Rudolph, and Martins, JoséC.

Abstract

The interaction between Ac‐AMP2, a lectin‐like small protein with antimicrobial and antifungal activity isolated from Amaranthus caudatus, and N,N′,N″‐triacetyl chitotriose was studied using 1H NMR spectroscopy. Changes in chemical shift and line width upon increasing concentration of N,N′,N″‐triacetyl chitotrioseto Ac‐AMP2 solutions at pH 6.9 and 2.4 were used to determine the interaction site and the association constant Ka. The most pronounced shifts occur mainly in the C‐terminal half of the sequence. They involve the aromatic residues Phe18, Tyr20and Tyr27together with their surrounding residues, as well as the N‐terminal Val‐Gly‐Glu segment. Several NOEs between Ac‐AMP2 and the N,N′,N″‐triacetyl chitotriose resonances are reported.

Published
1995
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