The Experts below are selected from a list of 2532 Experts worldwide ranked by ideXlab platform
J T Finch - One of the best experts on this subject based on the ideXlab platform.
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binding of the dye congo red to the amyloid protein Pig Insulin reveals a novel homology amongst amyloid forming peptide sequences
Journal of Molecular Biology, 1992Co-Authors: William G Turnell, J T FinchAbstract:Abstract The three-dimensional structure has been determined of a complex of the dye Congo Red, a specific stain for amyloid deposits, bound to the amyloid protein Insulin. One dye molecule intercalates between two globular Insulin molecules at an interface formed by a pair of anti-parallel β-strands. This result, together with analysis of the primary sequences of other amyloidogenic proteins and peptides suggests that this mode of dye-binding to amyloid could be general. Moreover, the structure of this dye-binding interface between protein molecules provides an insight into the polymerization of amyloidogenic proteins into amyloid fibres. Thus the detailed characterization, at a resolution of 2.5 A, of the dye binding site in Insulin could form a basis for the design of agents targeted against a variety of amyloid deposits.
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binding of the dye congo red to the amyloid protein Pig Insulin reveals a novel homology amongst amyloid forming peptide sequences
Journal of Molecular Biology, 1992Co-Authors: William G Turnell, J T FinchAbstract:The three-dimensional structure has been determined of a complex of the dye Congo Red, a specific stain for amyloid deposits, bound to the amyloid protein Insulin. One dye molecule intercalates between two globular Insulin molecules at an interface formed by a pair of anti-parallel beta-strands. This result, together with analysis of the primary sequences of other amyloidogenic proteins and peptides suggests that this mode of dye-binding to amyloid could be general. Moreover, the structure of this dye-binding interface between protein molecules provides an insight into the polymerization of amyloidogenic proteins into amyloid fibres. Thus the detailed characterization, at a resolution of 2.5 A, of the dye binding site in Insulin could form a basis for the design of agents targeted against a variety of amyloid deposits.
William G Turnell - One of the best experts on this subject based on the ideXlab platform.
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binding of the dye congo red to the amyloid protein Pig Insulin reveals a novel homology amongst amyloid forming peptide sequences
Journal of Molecular Biology, 1992Co-Authors: William G Turnell, J T FinchAbstract:Abstract The three-dimensional structure has been determined of a complex of the dye Congo Red, a specific stain for amyloid deposits, bound to the amyloid protein Insulin. One dye molecule intercalates between two globular Insulin molecules at an interface formed by a pair of anti-parallel β-strands. This result, together with analysis of the primary sequences of other amyloidogenic proteins and peptides suggests that this mode of dye-binding to amyloid could be general. Moreover, the structure of this dye-binding interface between protein molecules provides an insight into the polymerization of amyloidogenic proteins into amyloid fibres. Thus the detailed characterization, at a resolution of 2.5 A, of the dye binding site in Insulin could form a basis for the design of agents targeted against a variety of amyloid deposits.
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binding of the dye congo red to the amyloid protein Pig Insulin reveals a novel homology amongst amyloid forming peptide sequences
Journal of Molecular Biology, 1992Co-Authors: William G Turnell, J T FinchAbstract:The three-dimensional structure has been determined of a complex of the dye Congo Red, a specific stain for amyloid deposits, bound to the amyloid protein Insulin. One dye molecule intercalates between two globular Insulin molecules at an interface formed by a pair of anti-parallel beta-strands. This result, together with analysis of the primary sequences of other amyloidogenic proteins and peptides suggests that this mode of dye-binding to amyloid could be general. Moreover, the structure of this dye-binding interface between protein molecules provides an insight into the polymerization of amyloidogenic proteins into amyloid fibres. Thus the detailed characterization, at a resolution of 2.5 A, of the dye binding site in Insulin could form a basis for the design of agents targeted against a variety of amyloid deposits.
Ebbe Engholm - One of the best experts on this subject based on the ideXlab platform.
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expression receptor binding and biophysical characterization of guinea Pig Insulin desb30 a monomeric Insulin variant
ChemBioChem, 2015Co-Authors: Ebbe Engholm, Thomas H Hansen, Eva Johansson, Holger M Strauss, Tine N Vinther, Knud J Jensen, Frantisek Hubalek, Thomas KjeldsenAbstract:Here we report, for the first time, the heterologous expression of desB30 guinea Pig Insulin (GI desB30) in the yeast Saccharomyces cerevisiae. The affinities of GI desB30 for the Insulin receptor A and the IGF-I receptor were also quantified for the first time. Small-angle X-ray scattering and analytical ultracentrifugation studies confirmed that GI desB30 did not form dimers or hexamers, in contrast to human Insulin. Size-exclusion chromatography connected to inductively coupled plasma mass spectrometry revealed that GI desB30 has affinity towards several divalent metal ions. These studies did not indicate the formation of any larger structures of GI desB30 in the presence of various divalent metal ions, but did indicate that GI desB30 has an affinity towards Mn, Co, and Cu ions. Finally, the low affinity for the Insulin receptor and the very low affinity for the IGF-I receptor by GI desB30 were quantified.
Janos Ladik - One of the best experts on this subject based on the ideXlab platform.
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conformational influence on the hopping conductivity in Pig Insulin
Physical Review B, 1995Co-Authors: Janos LadikAbstract:The ac conductivity of Pig Insulin has been reported previously [Y.-J. Ye and J. Ladik, Phys. Rev. B 48, 5120 (1993); Int. J. Quantum Chem. 52, 491 (1994)]. Now we have calculated in the ab initio scheme using Clementi's minimal basis set and the random-walk theory of Lax and co-workers the ac conductivity in another conformation that occurs in the same crystal. The results confirm the conclusions of the previous papers, that is, native proteins can be good amorphous semiconductors if they are doped. The comparison of the results of the two conformations of Pig Insulin shows that the ac conductivity changes two orders of magnitude in the frequency range that corresponds to the time period of the elementary steps of chemical reactions (\ensuremath{\omega}g${10}^{10}$ ${\mathrm{sec}}^{\mathrm{\ensuremath{-}}1}$) when the three-dimensional structure changes. However, it does not change significantly in the low-frequency range (\ensuremath{\omega}${10}^{4}$ ${\mathrm{sec}}^{\mathrm{\ensuremath{-}}1}$). The conclusion is that in the high-frequency range Insulin would change both the ac conductivity of itself and its receptor if it binds to a receptor. Thus Insulin might change the electron transport in the receptor when it expresses its biological activity.
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Theory of hopping conductivity in Pig Insulin.
Physical review. B Condensed matter, 1993Co-Authors: Janos LadikAbstract:The ac conductivity for a native protein, Pig Insulin, was calculated in the ab initio scheme using Clementi's minimal basis set. The hopping centers and «main residue» of an orbital are defined. It is assumed that the hopping events of charge carriers happen among these centers of main residues. The analysis of primary hopping events shows that there might be a relationship between the distribution of the hopping centers and the biochemical activity of Insulin, and that the disulfur bridges of Insulin have particular relevance for the ac conduction. The formulas for calculation of the ac conductivity of proteins are given
Thomas Kjeldsen - One of the best experts on this subject based on the ideXlab platform.
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expression receptor binding and biophysical characterization of guinea Pig Insulin desb30 a monomeric Insulin variant
ChemBioChem, 2015Co-Authors: Ebbe Engholm, Thomas H Hansen, Eva Johansson, Holger M Strauss, Tine N Vinther, Knud J Jensen, Frantisek Hubalek, Thomas KjeldsenAbstract:Here we report, for the first time, the heterologous expression of desB30 guinea Pig Insulin (GI desB30) in the yeast Saccharomyces cerevisiae. The affinities of GI desB30 for the Insulin receptor A and the IGF-I receptor were also quantified for the first time. Small-angle X-ray scattering and analytical ultracentrifugation studies confirmed that GI desB30 did not form dimers or hexamers, in contrast to human Insulin. Size-exclusion chromatography connected to inductively coupled plasma mass spectrometry revealed that GI desB30 has affinity towards several divalent metal ions. These studies did not indicate the formation of any larger structures of GI desB30 in the presence of various divalent metal ions, but did indicate that GI desB30 has an affinity towards Mn, Co, and Cu ions. Finally, the low affinity for the Insulin receptor and the very low affinity for the IGF-I receptor by GI desB30 were quantified.