Results 251 to 260 of about 4,543,078 (309)
Synthesis, Thermal Stability, and Ionic Conductivity of Phenyl-Extended Viologen Ditriflate Salts: Tailoring Properties via Oxyethylene Chain Length. [PDF]
ACS OmegaCox SL +8 more
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Enhanced tunneling magnetoresistance and thermal stability in magnetic tunnel junctions with multiple CoFeB/Ta interfaces. [PDF]
Sci RepAmara S +4 more
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Tagged and untagged amyloid precursor protein E2 domain have comparable thermal stability and metal-ion binding propensity. [PDF]
BMC Res NotesNxele Z +4 more
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Thermal stability of the CuZrSe2
Journal of Solid State Chemistry, 2023The CuZrSe2 compound was synthesized for the first time by intercalation of Cu into the ZrSe2 lattice at room temperature. Experimental study of the thermal stability of CuZrSe2 has been performed by in-situ temperature-dependent synchrotron radiation X-ray diffraction (SR-XRPD). CuZrSe2 has a layered structure with space group P 3 m1. The copper atoms
Elena G. Shkvarina +7 more
openaire +2 more sources
Polymer/Montmorillonite Nanocomposites With Improved Thermal Properties: Part I. Factors Influencing Thermal Stability and Mechanisms of Thermal Stability Improvement [PDF]
Thermochimica Acta, 2007 The results of recent research indicate that the introduction of layered silicate – montmorillonite – into polymer matrix results in increase of thermal stability of a number of polymer nanocomposites.
James Njuguna +2 more
exaly +2 more sources
Archives of Biochemistry and Biophysics, 1973
Abstract The maximum melting points of 14 proteins in respect to pH are reported, the correlation coefficient between the hydrophobic index and the melting point was +0.622, and that between the average residue volumes and the melting points was +0.960.
H B, Bull, K, Breese
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Abstract The maximum melting points of 14 proteins in respect to pH are reported, the correlation coefficient between the hydrophobic index and the melting point was +0.622, and that between the average residue volumes and the melting points was +0.960.
H B, Bull, K, Breese
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2020
Proteins, in general, fold to a well-organized three-dimensional structure in order to function. The stability of this functional shape can be perturbed by external environmental conditions, such as temperature. Understanding the molecular factors underlying the resistance of proteins to the thermal stress has important consequences.
Sterpone, Fabio +2 more
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Proteins, in general, fold to a well-organized three-dimensional structure in order to function. The stability of this functional shape can be perturbed by external environmental conditions, such as temperature. Understanding the molecular factors underlying the resistance of proteins to the thermal stress has important consequences.
Sterpone, Fabio +2 more
openaire +3 more sources
Journal of Pharmaceutical Sciences, 2003
Worldwide vaccination programs against infectious diseases and toxins are estimated to save approximately 3 million lives yearly. Tragically, however, another 3 million individuals (primarily children) die of vaccine-preventable diseases. A significant portion of this problem results from the thermal instability of many of the currently used vaccines ...
Duane T, Brandau +4 more
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Worldwide vaccination programs against infectious diseases and toxins are estimated to save approximately 3 million lives yearly. Tragically, however, another 3 million individuals (primarily children) die of vaccine-preventable diseases. A significant portion of this problem results from the thermal instability of many of the currently used vaccines ...
Duane T, Brandau +4 more
openaire +2 more sources
Annals of the New York Academy of Sciences, 2006
Abstract: Protein stability is critical to the outcome of nearly all thermally mediated applications to biomaterials such as thermal therapies (including cryosurgery), burn injury, and biopreservation. As such, it is imperative to understand as much as possible about how a protein loses stability and to what extent we can control this through the ...
John C, Bischof, Xiaoming, He
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Abstract: Protein stability is critical to the outcome of nearly all thermally mediated applications to biomaterials such as thermal therapies (including cryosurgery), burn injury, and biopreservation. As such, it is imperative to understand as much as possible about how a protein loses stability and to what extent we can control this through the ...
John C, Bischof, Xiaoming, He
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Thermal stability and protein structure
Biochemistry, 1979Amino acid sequences have been compared for thermophilic and mesophilic molecules of ferredoxin, glyceraldehyde-3-phosphate dehydrogenase, and lactate dehydrogenase. It is shown that Gly, Ser, Ser, Lys, and Asp in mesophiles are generally substituted by Ala, Ala, Thr, Arg, and Glu, respectively, in thermophiles.
P, Argos +5 more
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