Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Abel Jonckheer"'
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 80:239-245
We have inserted a tryptophan (F77W) in the core of the regulatory domain of cardiac troponin C (cNTnC), and previously determined the structure of this mutant with and without the cosolvent trifluoroethanol (TFE). Interestingly, the orientations of
Autor:
Abel Jonckheer, Ann Gils, Erik Ceresa, Yves Engelborghs, Paul Declerck, M. De Maeyer, Miet Peeters
Publikováno v:
Journal of Thrombosis and Haemostasis. 5:2105-2112
Summary. Background: Activated thrombin activatable fibrinolysis inhibitor (TAFIa) plays a pivotal role in fibrinolysis. TAFIa activity is regulated by a temperature-dependent instability. This instability has not only complicated the study of struct
Autor:
Nina V. Visser, Yves Engelborghs, Anton J.W.G. Visser, Olaf Rolinsky, Marc De Maeyer, Abel Jonckheer, Jean-Marie Frère
Publikováno v:
Biophysical Journal. 100(3)
The fluorescence emission of the single tryptophan (W233) of the mutant protein DD carboxypeptidase from streptomyces is characterized by a red edge excitation shift (REES). This phenomenon is an indication for strongly reduced dynamics in the enviro
Publikováno v:
Current proteinpeptide science. 9(5)
We discuss the dynamics of tryptophan rotamers in the context of the non-exponential fluorescence decay in proteins. The central question is: how does the ground-state conformational heterogeneity influence the time evolution of tryptophan fluorescen
Publikováno v:
Biophysical Journal. 98:748a
Several NMR studies have shown that co-solvent trifluoroethanol (TFE) does not perturb the overall three-dimensional structure of proteins. We have inserted a single tryptophan (F77W) in the hydrophobic core of the N-domain of cardiac troponin C (cNT
Publikováno v:
Biophysical Journal. (6):1778-1786
The origin of the biexponential fluorescence decay of Trp in ribonuclease T1 under mildly destabilizing conditions, such as increased pH or temperature, or the presence of detergent, is still not understood. We have performed two extended replica-exc
Autor:
Jean-Marc Plesséria, Jean-Marie Zimmer, Abel Jonckheer, Kristel Van Laethem, Miguel E. Quiñones-Mateu, Marc De Maeyer, François Roman, Kris Covens, Jean-Claude Schmit, Anne-Mieke Vandamme, Jan Weber, Christine Lambert, Jean-Yves Servais, Ana C. Vazquez
Publikováno v:
ResearcherID
Summary: We observed an unusual glycine-to-glutamate substitution at protease (PR) residue position 48 (G48E) in an African patient infected with a subtype A1 HIV-1 strain failing a saquinavir-containing regimen. Phenotypic analysis of protease inhib
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