Multifractal properties of denaturation process based on Peyrard–Bishop model

2012 ◽  
Vol 376 (37) ◽  
pp. 2538-2547 ◽  
Author(s):  
S. Behnia ◽  
A. Akhshani ◽  
M. Panahi ◽  
A. Mobaraki ◽  
M. Ghaderian
Keyword(s):  
Denaturation Process

Simulation of a DNA denaturation process

2009 ◽  
Author(s):  
Tomas R. Ines ◽  
Francisco J. Cisneros ◽  
Angel Goni ◽  
Juan Castellanos
Keyword(s):  
Dna Denaturation ◽  
Denaturation Process

Denaturation of proteins. III. N.M.R. studies on lysozyme and α-lactalbumin

1971 ◽  
Vol 24 (8) ◽  
pp. 1703 ◽  
Author(s):  
JH Bradbury ◽  
NLR King
Keyword(s):  
Time Scale ◽  
High Field ◽  
Measured Parameter ◽  
Methionine Residue ◽  
Aromatic Interactions ◽  
Arginine Residues ◽  
Multiple State ◽  
Proton Resonances ◽  
Denaturation Of Proteins ◽  
Denaturation Process

The denaturation process is considered with particular reference to the application of N.M.R. spectroscopy for its study. All known examples of exchange between native and unfolded states are shown to be cases of slow exchange on the N.M.R. time scale. Furthermore, providing the denaturation is two-state, the fraction of unfolded molecules α can be obtained from measurements of the heights of various N.M.R. resonances, including those which are composites of several closely related types of protons. The experimentally measured parameter F does not equal α if intermediates are present or in the very unlikely event of the denaturation process occurring rapidly on the n.m.r, time scale. Multiple-state denaturations can be observed by the non-coincidence of curves of F (determined from different resonances) against denaturant parameter or from the occurrence of proton resonances which are only observed in the transition region. ��� Lysozyme is not denatured in 8M urea at pH > 3.0. At pH 2.8 the NH resonances of arginine sharpen before those of many other proton resonances in the molecule which sharpen simultaneously. It is concluded that three clusters of arginine side-chains, which involve seven arginine residues, unfold before the bulk of the molecule. Denaturation of α-lactalbumin in urea at pH 2.5 and pH 6.0 in D2O occurs over a broad range of concentrations and is clearly multiple state at pH 6.0. ��� The N.M.R. study shows the presence of an exposed methionine residue in α-lactalbumin, no evidence of high field perturbed methyl resonances, and a considerably reduced stability to denaturation as compared with lysozyme. The dearth of aliphatic-aromatic interactions in α-lactalbumin may account for its more open structure compared with lysozyme as well as its reduced stability towards denaturation.

scholarly journals Molecular mechanism for thermal denaturation of thermophilic rhodopsin

2019 ◽  
Vol 10 (31) ◽  
pp. 7365-7374 ◽  
Author(s):  
Ramprasad Misra ◽  
Amiram Hirshfeld ◽  
Mordechai Sheves
Keyword(s):  
Schiff Base ◽  
Molecular Mechanism ◽  
Thermal Denaturation ◽  
Rate Determining Step ◽  
Hydrolysis Of ◽  
Denaturation Process

Studies of microbial rhodopsins revealed that hydrolysis of the retinal protonated Schiff base is the rate-determining step of the thermal denaturation process.

scholarly journals Studies on Denaturation Process of Fish Myosin.

1999 ◽  
Vol 65 (3) ◽  
pp. 382-385
Author(s):  
Kunihiko Konno
Keyword(s):  
Denaturation Process

Effects of monopropanediamino-β-cyclodextrin on the denaturation process of the hybrid protein BlaPChBD

2011 ◽  
Vol 1814 (9) ◽  
pp. 1146-1153 ◽  
Author(s):  
Marylène Vandevenne ◽  
Gilles Gaspard ◽  
El Mustapha Belgsir ◽  
Manilduth Ramnath ◽  
Yves Cenatiempo ◽  
...  
Keyword(s):  
Hybrid Protein ◽  
Denaturation Process

Study of the Denaturation Process in Albumin−Urea Solutions by Means of the Thermally Stimulated Depolarization Currents Technique

1996 ◽  
Vol 100 (5) ◽  
pp. 1914-1917 ◽  
Author(s):  
A. Vassilikou-Dova ◽  
S. Grigorakakis ◽  
P. Varotsos ◽  
A. Kapetanaki ◽  
D. Koutsikos
Keyword(s):  
Thermally Stimulated Depolarization ◽  
Denaturation Process
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