Temperature effects proteins

Andersen, J.N., "Temperature Effect on Recombinant Protein Production Using a Baculovirus/Insect Cell Expression System", Diploma Thesis, University of Calgary and Technical University of Denmark, 1995. 

Cohen, K. A., Schellenberg, K., Benedek, K., Karger, B. L., Grego, B., and Hearn, M. T. W., Mobile-phase and temperature effects in the reversed phase chromatographic separation of proteins, Anal. Biochem., 140, 223, 1984. 

Le Bellego L, Van Milgen J and Noblet J (2002), Effect of high ambient temperature on protein and lipid deposition and energy utilization in growing pigs , Anim Sci, 75, 85-96. 

Cosolvent and temperature effects on various types of noncovalent forces involved in protein-protein interactions are now well documented. These effects have been intensively studied in Douzou s laboratory through their impact on protein fractionation (Douzou and Balny, 1978). Mixed solvents at carefully controlled concentration and temperature variations in the range of normal and subzero temperatures ap-... 

Temperature and pH effects on hemopexin, its domains, and the respective heme complexes have also been examined using absorbance and CD spectroscopy, which reflect stability of the heme iron-bis-histidyl coordination of hemopexin and of the conformation of protein, rather than overall thermodynamic unfolding of the protein. Using these spectral methods to follow temperature effects on hemopexin stability yielded results generally comparable to the DSC findings, but also revealed interesting new features (Fig. 14) (N. Shipulina et al., unpublished). Melting experiments showed that apo-hemopexin loses tertiary... 

Effective ligand rebinding from the Xel site is only observed when the temperature has risen above a characteristic temperature 180 K (Figure 1.6), which is the temperature where protein dynamics sets in. However, the time-related information is lost in experiments at cryogenic temperatures. Time-resolved crystallography was applied to restore the time scale and observe undisturbed relaxations. 

They also found that at 1O8 C protein aggregation occurred, probably as a result of disulfide bond formation, and they suggested that this effect might provide an alternative to chemical oxidation for dough improvement. At higher temperatures, the protein aggregates broke down. The authors postulated that at the higher temperatures not only... 

Particularly interesting seems to be the conclusion of Schreck and Ludwig [27], who hypothesized that the barometric resistance of micro-organisms is caused by a mechanical factor, but is also dependent upon the protein-structure of microbes, as there is a deep relationship between the effect of pressure and temperature on proteins and micro-organisms. In other words, pressure acts on proteins located in specific sites where they are particularly sensitive to mechanical stress. 

The magnetic susceptibility measurements of (159) show a molecular paramagnetism in the reduced protein characteristic of a S=l/2 compound. The absence of internal magnetic effects in the high-temperature, reduced-protein spectra are explained by the Mossbauer spectra shown in Fig. 10. 

Haschemeyer, A.E.V. (1980). Temperature effects on protein metabolism in cold-adapted fishes. Antarctic Journal of the United States 15,147-149. 

Haschemeyer, A.E.V., Persell, R. and Smith, M.A.K. (1979). Effect of temperature on protein synthesis in fish of the Galapagos and Perlas Islands. Comparative Biochemistry and Physiology 64B, 91-95. 

The effect of temperature satisfies the Arrhenius relationship where the applicable range is relatively small because of low and high temperature effects. The effect of extreme pH values is related to the nature of enzymatic proteins as polyvalent acids and bases, with acid and basic groups (hydrophilic) concentrated on the outside of the protein. Finally, mechanical forces such as surface tension and shear can affect enzyme activity by disturbing the shape of the enzyme molecules. Since the shape of the active site of the enzyme is constructed to correspond to the shape of the substrate, small alteration in the structure can severely affect enzyme activity. Reactor s stirrer speed, flowrate, and foaming must be controlled to maintain the productivity of the enzyme. Consequently, during experimental investigations of the kinetics enzyme catalyzed reactions, temperature, shear, and pH are carefully controlled the last by use of buffered solutions. 

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