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Original scientific paper

Probing Protein Stability with Non-natural Amino Acids

Nediljko Budisa ; Max-Planck Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried, Germany
Greta Pifat ; Ruđer Bošković Institute, Bijenička 54, 10001 Zagreb, Croatia

Fulltext: english, pdf (121 KB) pages 179-187 downloads: 177* cite
APA 6th Edition
Budisa, N. & Pifat, G. (1998). Probing Protein Stability with Non-natural Amino Acids. Croatica Chemica Acta, 71 (1), 179-187. Retrieved from https://hrcak.srce.hr/132334
MLA 8th Edition
Budisa, Nediljko and Greta Pifat. "Probing Protein Stability with Non-natural Amino Acids." Croatica Chemica Acta, vol. 71, no. 1, 1998, pp. 179-187. https://hrcak.srce.hr/132334. Accessed 23 Nov. 2019.
Chicago 17th Edition
Budisa, Nediljko and Greta Pifat. "Probing Protein Stability with Non-natural Amino Acids." Croatica Chemica Acta 71, no. 1 (1998): 179-187. https://hrcak.srce.hr/132334
Harvard
Budisa, N., and Pifat, G. (1998). 'Probing Protein Stability with Non-natural Amino Acids', Croatica Chemica Acta, 71(1), pp. 179-187. Available at: https://hrcak.srce.hr/132334 (Accessed 23 November 2019)
Vancouver
Budisa N, Pifat G. Probing Protein Stability with Non-natural Amino Acids. Croatica Chemica Acta [Internet]. 1998 [cited 2019 November 23];71(1):179-187. Available from: https://hrcak.srce.hr/132334
IEEE
N. Budisa and G. Pifat, "Probing Protein Stability with Non-natural Amino Acids", Croatica Chemica Acta, vol.71, no. 1, pp. 179-187, 1998. [Online]. Available: https://hrcak.srce.hr/132334. [Accessed: 23 November 2019]

Abstracts
Quantitative replacement of methionine with its non-natural amino acid analogues, norleucine, selenomethionine and telluromethionine in human recombinant annexin V, is applied to study conformational and folding properties in solution. This procedure replaces each methionine sulphur atom with Se, Te or -CH2-, providing single-atom exchanges, or »atomic mutations«. Using guanidine chloride as denaturant, the estimated stabilities of protein variants are not significantly changed. The denaturation midpoints are shifted towards lower values owing to the increase in the hydrophobicity of exchanged residues. Co-operativity expressed in terms of m-values is also affected by such exchanges and is highly correlated with the physical properties of methionine and its analogues in solution. This approach can contribute to a detailed understanding of interactions of particular amino acids and their implications on protein folding and protein-ligand interactions.

Hrčak ID: 132334

URI
https://hrcak.srce.hr/132334

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