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

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.

scholarly journals Domain swapping of a llama VHH domain builds a crystal-wide β-sheet structure

FEBS Letters ◽  
2004 ◽  
Vol 564 (1-2) ◽  
pp. 35-40 ◽  
Author(s):  
Silvia Spinelli ◽  
Aline Desmyter ◽  
Leon Frenken ◽  
Theo Verrips ◽  
Mariella Tegoni ◽  
...  
Keyword(s):  
Domain Swapping ◽  
Sheet Structure ◽  
Β Sheet

Laser Raman Spectroscopic Study Of The β-Sheet Structure Of Fibrinx

1981 ◽  
Author(s):  
J Marx ◽  
G Hudry-Clergeon ◽  
L Bernard
Keyword(s):  
Protein Conformation ◽  
Protein Concentration ◽  
Structural Changes ◽  
Fibre Diameter ◽  
Enzymatic Conversion ◽  
Raman Spectroscopic ◽  
Laser Raman ◽  
Sheet Structure ◽  
Two Parameters ◽  
Β Sheet

Raman spectroscopy has proved to be a useful tool in the study of protein conformation in aqueous solution. Structural changes have been observed by this technique during the enzymatic conversion of fibrinogen into fibrin (J. Marx and col. (1979) Biochim. Biophys. Acta., 578, 107-115), particularly by the study of the Amide I and Amide III regions an important increase in the β-sheet form has been shown to occur. This variation is investigated under various conditions of ionic strength (μ) and protein concentration (c), two parameters which are known to change the fibre diameter (low values of μ and c favor an increase in the fibre diameter). The amount of β-sheet structure in fibrinogen is approximately 10 % and is unaffected by μ or c. In fibrin, the amount of β-sheet increases progressively from 20 % in fine clots (low diameter fibres) to more than 30 % in coarse clots (high diameter fibres). This correlation between the percentage of β-sheet structure and fibre diameter in fibrin indicates that numerous intermonomer hydrogen bonds are formed in the equatorial direction of the fibre. These bonds would greatly consolidate the association between monomers which is probably initiated at a few highly specific sites.

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