An <i>In silico</i> analysis on the phosphorylation dependent structural and thermal stability of thermophilic proteins. [PDF]
Arunachalam S, Gnanasekaran R.
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Modification of Whey Protein Isolate with Surfactants Based on Hofmeister Series and Interaction Parameter. [PDF]
Lopes JS +2 more
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Processing-Induced Modifications of Camel Milk Immunoglobulins and Lactoferrin: Implications for Immunocompromised Pediatric Populations and Therapeutic Applications. [PDF]
Alhaj OA +3 more
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The Influence of Harmonic Ratio on HIFU-Induced Thermal Lesion Formation in Biological Tissue. [PDF]
Dong H, Hu J, Chen W.
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Tracking Protein Misfolding and Oligomerization: A Temperature-Controlled Ion Mobility-Mass Spectrometry Approach. [PDF]
Svingou D +3 more
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Thermal Fluctuations in Histone During Denaturation [PDF]
In this paper, we address the issue of thermal fluctuations during the thermal denaturation of linker histone H1 which is the basic ingredient of chromatin assembly. We measure the thermal fluctuations using a sensitive nanocalorimeter based thermal fluctuation measurement set up which can measure fluctuations of the order of 1 part per billion.
Nagapriya, KS +2 more
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Thermal denaturation of staphylococcal nuclease
Biochemistry, 1985The fully reversible thermal denaturation of staphylococcal nuclease in the absence and presence of Ca2+ and/or thymidine 3',5'-diphosphate (pdTp) from pH 4 to 8 has been studied by high-sensitivity differential scanning calorimetry. In the absence of ligands, the denaturation is accompanied by an enthalpy change of 4.25 cal g-1 and an increase in ...
R O, Calderon +3 more
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Thermal denaturation of subchromosomal particles
Biochemical and Biophysical Research Communications, 1975Summary Monomer chromatin subunits prepared by micrococcal nuclease digestion showed a monophasic thermal denaturation transition with a Tm of about 77°C. By contrast, dimers and higher oligomers gave a biphasic melting profile, with Tms at 45–55°C and 77°C.
C L, Woodcock, L L, Frado
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Nonideality and protein thermal denaturation
Biopolymers, 1999We studied the thermal denaturation of eglin c by using CD spectropolarimetry and differential scanning calorimetry (DSC). At low protein concentrations, denaturation is consistent with the classical two-state model. At concentrations greater than several hundred microM, however, the calorimetric enthalpy and the midpoint transition temperature ...
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