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A thermal shift assay quantifies the change in thermal denaturation temperature of a protein under varying conditions. The differing conditions that can be examined are very diverse, e.g. pH, salts, additives, drugs, drug leads, oxidation/reduction, or mutations. The binding of low molecular weight ligands can increase the thermal stability of a protein, as described by Koshland (1958)^[1] and Linderstrom-Lang and Schellman (1959).^[2]. Almost half of enzymes require a metal ion co-factor^[3]. Thermostable proteins are often more useful than their non-thermostable counterparts, e.g. DNA polymerase in the polymerase chain reaction^[4], protein engineering often includes

^ Koshland, DE (February 1958). "Application of a Theory of Enzyme Specificity to Protein Synthesis". Proceedings of the National Academy of Sciences of the United States of America. 44 (2): 98–104. PMID 16590179.
^ Linderstrøm-Lang, K., and Schellman, J. A. (1959). "Protein structure and enzyme activity". The Enzymes. 1(2) 443-510.
^ Waldron, KJ; Rutherford, JC; Ford, D; Robinson, NJ (13 August 2009). "Metalloproteins and metal sensing". Nature. 460 (7257): 823–30. PMID 19675642.
^ Saiki, RK; Gelfand, DH; Stoffel, S; Scharf, SJ; Higuchi, R; Horn, GT; Mullis, KB; Erlich, HA (29 January 1988). "Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase". Science (New York, N.Y.). 239 (4839): 487–91. PMID 2448875.

[1] Koshland, DE (February 1958). "Application of a Theory of Enzyme Specificity to Protein Synthesis". Proceedings of the National Academy of Sciences of the United States of America. 44 (2): 98–104. PMID 16590179.

[2] Linderstrøm-Lang, K., and Schellman, J. A. (1959). "Protein structure and enzyme activity". The Enzymes. 1(2) 443-510.

[3] Waldron, KJ; Rutherford, JC; Ford, D; Robinson, NJ (13 August 2009). "Metalloproteins and metal sensing". Nature. 460 (7257): 823–30. PMID 19675642.

[4] Saiki, RK; Gelfand, DH; Stoffel, S; Scharf, SJ; Higuchi, R; Horn, GT; Mullis, KB; Erlich, HA (29 January 1988). "Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase". Science (New York, N.Y.). 239 (4839): 487–91. PMID 2448875.

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