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文章詳情
Literature references of Chirascan CD Spectrometer employed to characterize
日期：2023-01-28 00:35
瀏覽次數：4586
摘要：
Small organic molecule binding
o Acetylphosphinate is the most potent mechanism-basedsubstrate-like inhibitor of both the human and
E. coli pyruvate dehydrogenase components of the pyruvatedehydrogenase complex.
Natalia S. Nemeria, Lioubov G. Korotchkina, Sumit Chakraborty,Mulchand S. Patel and Frank Jordan
Bioorg Chem. 2006 December; 34(6): 362–379.
o THE PUZZLE OF LIGANDS BINDING TO Corynebacterium ammoniagenes FADSYNTHETASE
Susana Frago, Adrián Velázquez-Campoy and Milagros Medina
J. Biol. Chem., Vol. 284, Issue 11, 6610-6619, March 13, 2009
Metal binding
o Biochemical and spectroscopic studies of human melanotransferrin(MTf): Electron-paramagnetic
resonance evidence for a difference between the iron-binding siteof MTf and other transferrins
Sebastien Farnauda, Maryam Aminib, Chiara Rapisardab, RichardCammackc, Tam Buic, Alex Drakec,
Robert W. Evansd, Yohan Suryo Rahmantoe and Des R. Richardson
The International Journal of Biochemistry & Cell Biology
Volume 40, Issue 12, 2008, Pages 2739-2745
Almost all of John Viles Chirascan papers involve using theChirascan to study binding of various metals to
prion proteins. Among a number of papers:
o Fragment length influences affinity for Cu2+ and Ni2+ binding toHis96 or His111 of the prion protein and
spectroscopic evidence for a multiple histidine binding only at lowpH
Mark Klewpatinond and John H. Viles
Biochem J. 2007 June 15; 404(Pt 3): 393–402. Published online 2007May 29. Prepublished online
2007 March 2. doi: 10.1042/BJ20061893.
Also include the diazepam/ibuprofen binding.
o Deconvoluting the Cu2+ Binding Modes of Full-length PrionProtein.
Mark Klewpatinond, Paul Davies, Suzanne Bowen, David R. Brown, andJohn H. Viles.
J. Biol. Chem., Vol. 283, Issue 4, 1870-1881, January 25, 2008
o Acetylphosphinate is the most potent mechanism-basedsubstrate-like inhibitor of both the human and
E. coli pyruvate dehydrogenase components of the pyruvatedehydrogenase complex.
Natalia S. Nemeria, Lioubov G. Korotchkina, Sumit Chakraborty,Mulchand S. Patel and Frank Jordan
Bioorg Chem. 2006 December; 34(6): 362–379.
o THE PUZZLE OF LIGANDS BINDING TO Corynebacterium ammoniagenes FADSYNTHETASE
Susana Frago, Adrián Velázquez-Campoy and Milagros Medina
J. Biol. Chem., Vol. 284, Issue 11, 6610-6619, March 13, 2009
Metal binding
o Biochemical and spectroscopic studies of human melanotransferrin(MTf): Electron-paramagnetic
resonance evidence for a difference between the iron-binding siteof MTf and other transferrins
Sebastien Farnauda, Maryam Aminib, Chiara Rapisardab, RichardCammackc, Tam Buic, Alex Drakec,
Robert W. Evansd, Yohan Suryo Rahmantoe and Des R. Richardson
The International Journal of Biochemistry & Cell Biology
Volume 40, Issue 12, 2008, Pages 2739-2745
Almost all of John Viles Chirascan papers involve using theChirascan to study binding of various metals to
prion proteins. Among a number of papers:
o Fragment length influences affinity for Cu2+ and Ni2+ binding toHis96 or His111 of the prion protein and
spectroscopic evidence for a multiple histidine binding only at lowpH
Mark Klewpatinond and John H. Viles
Biochem J. 2007 June 15; 404(Pt 3): 393–402. Published online 2007May 29. Prepublished online
2007 March 2. doi: 10.1042/BJ20061893.
Also include the diazepam/ibuprofen binding.
o Deconvoluting the Cu2+ Binding Modes of Full-length PrionProtein.
Mark Klewpatinond, Paul Davies, Suzanne Bowen, David R. Brown, andJohn H. Viles.
J. Biol. Chem., Vol. 283, Issue 4, 1870-1881, January 25, 2008
