Temperature, effect on protein

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

Dvorsky, R., Sevcik, J., Caves, L. S. D., Hubbard, R.E., and Verma, C. S. (2000) Temperature effect on protein motion a molecular dynamics study of RNAase-Sa/. Phys. Chem. B 104, 10387-10397. 

Pressure - Temperature Effects on Protein Conformational States... 

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. 

This process of cross-linking does not appear have a major effect on protein secondary structure at room temperature. However, cross-links formed by reactions of formaldehyde with proteins retard, but do not eliminate, protein denaturation that occurs when proteins are heated to a temperature of approximately 70°C or above.7... 

Note Some protocols avoid a reduction step, as it can lead to disulfide bond cleavage and detrimental effects on protein activity. As an alternative to reduction, add 50 pi of 0.2 M lysine in 0.5 M sodium carbonate, pH 9.5 to each ml of the conjugation reaction to block excess reactive sites. Block for 2 hours at room temperature. Other amine-containing small molecules may be substituted for lysine—such as glycine, Tris buffer, or ethanolamine. 

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generally comparable to the DSC findings, but also revealed interesting new features (Fig. 14) (N. Shipulina et al., unpublished).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... 

We have examined the effect of temperature and enzymes and other materials on the spectrum of the membrane fragment (4). As the temperature increases up to 120°C. the lipid chain [CH2]n signal becomes more prominent, suggesting that, at lower temperatures, the polymethylene chain is somehow inhibited in its molecular freedom. Treatment with phospholipase C removes the peak at 6.7t which we associate with the choline protons. Urea, which is known to have an unfolding effect on proteins, produces new peaks in the spectrum of the membrane which can be assigned to some of the constituent amino acids of the protein. There is, however, no marked increase in the polymethylene chain signal. The effect of trifluoroacetic acid on the membrane is to increase the intensity of the peak associated with the constituent amino acids of the protein, and now the polymethylene chain of the lipid is also clearly visible. 

The retention caused by different salts in equal concentration is in accordance with the Hofmeister series. The higher the molar surface tension increment of a salt, the greater is its effect on protein retention 55). Higher column temperatures produce prolonged retention in HIC, in contrast to RPC where retention decreases with increasing temperature56). 

To summarize, studies of differently thermally adapted confamilial, congeneric, and con-specific organisms have shown that temperature differences of a few degrees Celsius have sufficient effects on proteins to favor adaptive change. Although studies to date have focused on only a few classes of proteins, the ubiquitous effects of temperature on protein conformation are such that many, and perhaps most, proteins are likely to exhibit a similar threshold for perturbation and adaptive change. 

B. R. Brooks and P. J. Steinbach, Workshop on High Performance Computing and Grand Challenges in Structural Biology, Florida State University, Tallahassee, FL, Jan. 24—27, 1992. Temperature and Environmental Effects on Protein Dynamics, Comparisons of Mo-... 

Patten F, Gordy W. Temperature effects on free radical formation and electron migration in irradiated proteins. Proc. Natl. Acad. Sci. U.S.A. 1960 46 1137-1144. 

Effect on Proteins Proteins are denatured by the cooking process, an effect related to the temperature created. Proteins are made up of amino acids, which are known as the building blocks of protein. Amino acids are held together by primary bonds, whereas the molecules are held together by secondary bonds. The cooking action of the extruder breaks down the secondary bonds, but does not create sufficient heat to destroy the amino acids or the primary bonds. 

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