Chemical and thermal stability of insulin: effects of zinc and ligand binding to the insulin zinc-hexamer.
作者： Kasper Huus , Svend Havelund , Helle B. Olsen , Marco van de Weert , Sven Frokjaer
DOI: 10.1007/S11095-006-9098-Y
关键词: Random hexamer 、 Zinc 、 Insulin 、 Insulin receptor substrate 、 Thermal stability 、 Calorimetry 、 Biophysics 、 Deamidation 、 Chemistry 、 Chemical stability 、 Biochemistry
摘要: Purpose To study the correlation between thermal and chemical stability of insulin formulations with various hexamer ligands.
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sci-hub.se 参考文章(45)
T. V. BRENNAN, S. CLARKE, Deamidation and Isoaspartate Formation in Model Synthetic Peptides: The Effects of Sequence and Solution Environment ChemInform. ,vol. 26, ,(1995) , 10.1002/CHIN.199532300
Kasper Huus, Svend Havelund, Helle B. Olsen, Marco van de Weert, Sven Frokjaer, Thermal Dissociation and Unfolding of Insulin Biochemistry. ,vol. 44, pp. 11171- 11177 ,(2005) , 10.1021/BI0507940
Qing-xin Hua, Michael A. Weiss, Mechanism of insulin fibrillation: the structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate Journal of Biological Chemistry. ,vol. 279, pp. 21449- 21460 ,(2004) , 10.1074/JBC.M314141200
Jose Goldman, Frederick H. Carpenter, Zinc binding, circular dichroism, and equilibrium sedimentation studies on insulin (bovine) and several of its derivatives. Biochemistry. ,vol. 13, pp. 4566- 4574 ,(1974) , 10.1021/BI00719A015
Liza Nielsen, Ritu Khurana, Alisa Coats, Sven Frokjaer, Jens Brange, Sandip Vyas, Vladimir N. Uversky, Anthony L. Fink, Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism Biochemistry. ,vol. 40, pp. 6036- 6046 ,(2001) , 10.1021/BI002555C
Wonjae E. Choi, Mark L. Brader, Valentin Aguilar, Niels C. Kaarsholm, Michael F. Dunn, The allosteric transition of the insulin hexamer is modulated by homotropic and heterotropic interactions. Biochemistry. ,vol. 32, pp. 11638- 11645 ,(1993) , 10.1021/BI00094A021
Peter S. Brzovic, Wonjae E. Choi, Dan Borchardt, Niels C. Kaarsholm, Michael F. Dunn, Structural Asymmetry and Half-Site Reactivity in the T to R Allosteric Transition of the Insulin Hexamer Biochemistry. ,vol. 33, pp. 13057- 13069 ,(1994) , 10.1021/BI00248A015
Niels C. Kaarsholm, Hui Chong Ko, Michael F. Dunn, Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin, and miniproinsulin Biochemistry. ,vol. 28, pp. 4427- 4435 ,(1989) , 10.1021/BI00436A046
A. Kossiakoff, Tertiary structure is a principal determinant to protein deamidation. Science. ,vol. 240, pp. 191- 194 ,(1988) , 10.1126/SCIENCE.3353715
E. Hardin Strickland, Dan Mercola, Near-ultraviolet tyrosyl circular dichroism of pig insulin monomers, dimers, and hexamers. Dipole-dipole coupling calculations in the monopole approximation. Biochemistry. ,vol. 15, pp. 3875- 3884 ,(1976) , 10.1021/BI00662A035