Salt Dependence Conformational Stability of the Dimeric SAM Domain of MAPKKK Ste11 from Budding Yeast: A Native-State H/D Exchange NMR Study

Biochemistry ◽  
2020 ◽  
Vol 59 (31) ◽  
pp. 2849-2858
Author(s):  
Anirban Bhunia ◽  
Humaira Ilyas ◽  
Surajit Bhattacharjya
Life ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 652
Author(s):  
Serena Cozzolino ◽  
Attila Tortorella ◽  
Pompea Del Vecchio ◽  
Giuseppe Graziano

The conformational stability of globular proteins is strongly influenced by the addition to water of different co-solutes. Some of the latter destabilize the native state, while others stabilize it. It is emerging that stabilizing agents are able to counteract the action of destabilizing agents. We have already provided experimental evidence that this counteraction is a general phenomenon and offered a rationalization. In the present work, we show that four different sugars, namely fructose, glucose, sucrose, and trehalose, counteract the effect of urea, tetramethylurea, sodium perchlorate, guanidinium chloride, and guanidinium thiocyanate despite the chemical and structural differences of those destabilizing agents. The rationalization we provide is as follows: (a) the solvent-excluded volume effect, a purely entropic effect, stabilizes the native state, whose solvent-accessible surface area is smaller than the one of denatured conformations; (b) the magnitude of the solvent-excluded volume effect increases markedly in ternary solutions because the experimental density of such solutions is larger than that of pure water.


Biochemistry ◽  
2008 ◽  
Vol 47 (2) ◽  
pp. 651-659 ◽  
Author(s):  
Anirban Bhunia ◽  
Prerna N. Domadia ◽  
Xiaolong Xu ◽  
Richard Gingras ◽  
Feng Ni ◽  
...  

2010 ◽  
Vol 24 (3-4) ◽  
pp. 297-301 ◽  
Author(s):  
R. Bedotti ◽  
M. G. Bridelli ◽  
R. Capelletti ◽  
E. Polverini

The water molecules surrounding proteins as a thin layer and those packaged in pockets and cavities shape and control their structure. Thermally Stimulated Depolarization Currents (TSDC) technique has been applied to investigate the hydration structure of six proteins with different structural motifs: pepsin,β-lactoglobulin,α-chymotrypsin, bovine serum albumin, human serum albumin and myoglobin, at very low hydration level (water vapor activity aw≈0.80) both in the native state and after treatment in trifluoroethanol/water mixture 80% (v/v). A combined approach based on the use of the TSDC technique, able to distinguish H2O dipoles belonging to the solvation shell in terms of their order degree and mobility, and of FTIR and CD spectroscopies has allowed us to reexamine the problem of conformational stability of macromolecules as a function of their hydration.


2008 ◽  
Vol 75 (1) ◽  
pp. 40-52 ◽  
Author(s):  
P. M. Krishna Mohan ◽  
Swagata Chakraborty ◽  
Ramakrishna V. Hosur

Author(s):  
Masako Osumi ◽  
Misuzu Nagano ◽  
Hiroko Kazama

We have found that microbodies appeared profusely together with a remarkable increase in catalase activity in normal alkane-grown cells of hydrocarbon-utilizing Candida yeasts, and that the microbodies multiplied by division in these cells. These features of Candida yeasts seem to provide a useful model system for studies on the biogenesis of the microbody. Subsequently, we have succeeded in isolation of Candida microbodies in an apparently native state, as judged biochemically and morphologically. The presence of DNA in the purified microbody fraction thus obtained was proved by the diphenylamine method. DNA molecule of about 15 urn in contour length was released from an isolated microbody. The physicochemical analyses of the microbody DNA revealed that its buoyant density differed from nuclear and mitochondrial DNAs. All these results lead us to the possibility that there is a novel type of DNA in microbodies.


Author(s):  
Tokio Nei ◽  
Haruo Yotsumoto ◽  
Yoichi Hasegawa ◽  
Yuji Nagasawa

In order to observe biological specimens in their native state, that is, still containing their water content, various methods of specimen preparation have been used, the principal two of which are the chamber method and the freeze method.Using its recently developed cold stage for installation in the pre-evacuation chamber of a scanning electron microscope, we have succeeded in directly observing a biological specimen in its frozen state without the need for such conventional specimen preparation techniques as drying and metallic vacuum evaporation. (Echlin, too, has reported on the observation of surface structures using the same freeze method.)In the experiment referred to herein, a small sliced specimen was place in the specimen holder. After it was rapidly frozen by freon cooled with liquid nitrogen, it was inserted into the cold stage of the specimen chamber.


Author(s):  
Tomasz J. Idzik ◽  
Zofia M. Myk ◽  
Łukasz Struk ◽  
Magdalena Perużyńska ◽  
Gabriela Maciejewska ◽  
...  

Triisopropylsilyltrifluoromethanesulfonate can be effectively used for the arylation of a wide range of enelactams. The multinuclear NMR study provided deep insights into the reaction mechanism.


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