scholarly journals Exploring β-Sheet Structure and Interactions with Chemical Model Systems

2008 ◽  
Vol 41 (10) ◽  
pp. 1319-1330 ◽  
Author(s):  
James S. Nowick
Keyword(s):  
Model Systems ◽  
Chemical Model ◽  
Sheet Structure ◽  
Β Sheet

On the roles of the alanine and serine in the β-sheet structure of fibroin

2015 ◽  
Vol 197 ◽  
pp. 10-17 ◽  
Author(s):  
Juan Francisco Carrascoza Mayen ◽  
Alexandru Lupan ◽  
Ciprian Cosar ◽  
Attila-Zsolt Kun ◽  
Radu Silaghi-Dumitrescu
Keyword(s):  
Sheet Structure ◽  
Β Sheet

Effect of curcumin on amyloidogenic property of molten globule-like intermediate state of 2,5-diketo-d-gluconate reductase A

2009 ◽  
Vol 390 (10) ◽  
Author(s):  
Nandini Sarkar ◽  
Abhay Narain Singh ◽  
Vikash Kumar Dubey
Keyword(s):  
Protein Concentration ◽  
Molten Globule ◽  
Molar Ratio ◽  
Amyloid Formation ◽  
Molten Globule State ◽  
Force Microscopy ◽  
Atomic Force ◽  
Sheet Structure ◽  
Amyloid Diseases ◽  
Β Sheet

Abstract We identified a molten globule-like intermediate of 2,5-diketo-d-gluconate reductase A (DKGR) at pH 2.5, which has a prominent β-sheet structure. The molten globule state of the protein shows amyloidogenic property >50 μm protein concentration. Interestingly, a 1:1 molar ratio of curcumin prevents amyloid formation as shown by the Thioflavin-T assay and atomic force microscopy. To the best of our knowledge, this is the first report on amyloid formation by an (α/β)8-barrel protein. The results presented here indicate that the molten globule state has an important role in amyloid formation and potential application of curcumin in protein biotechnology as well as therapeutics against amyloid diseases.

Conformations of calf thymus and rye histones H3 and H4 in aqueous solution by laser Raman spectroscopy

1980 ◽  
Vol 58 (8) ◽  
pp. 633-640 ◽  
Author(s):  
M. Pézolet ◽  
R. Savoie ◽  
J.-G. Guillot ◽  
M. Pigeon-Gosselin ◽  
D. Pallotta
Keyword(s):  
Laser Raman Spectroscopy ◽  
Carboxylate Group ◽  
Weakly Bound ◽  
Tyrosine Residues ◽  
Laser Raman ◽  
Calf Thymus ◽  
Sheet Structure ◽  
High Degree ◽  
Β Sheet ◽  
Positively Charged

The Raman spectra of aqueous solutions of histones H3 and H4 from calf thymus and from rye reflect the high degree of conservation from species to species of the primary and secondary structures of these proteins. The amount of β-sheet structure is estimated at 40 ± 5% in H4 and at 33 ± 5% in H3 from the intensities of the amide I and amide III bands at 1663 and 1241 cm−1, respectively, in the spectra. These values are independent of the salt concentration of the solutions, most likely because of the high histone concentration (~3 mM) required to obtain the spectra, which results in some aggregation of the proteins. The intensity ratio of the tyrosine doublet at 852 and 826 cm−1 indicates that the four tyrosine residues in H4 are relatively exposed to the solvent or weakly bound to positively charged groups of basic amino acids, whereas in H3 at least one tyrosine is buried inside the protein and tightly bound to a carboxylate group. The results also show that the secondary structure of H3 is slightly influenced by the state of oxidation of the two cysteine residues it contains.

Increasing and Stabilizing β-Sheet Structure of Maize Zein Causes Improvement in Its Rheological Properties

2012 ◽  
Vol 60 (9) ◽  
pp. 2316-2321 ◽  
Author(s):  
Carla D. Mejia ◽  
David C. Gonzalez ◽  
Lisa J. Mauer ◽  
Osvaldo H. Campanella ◽  
Bruce R. Hamaker
Keyword(s):  
Rheological Properties ◽  
Sheet Structure ◽  
Β Sheet
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