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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

Puni tekst: engleski, pdf (121 KB) str. 179-187 preuzimanja: 177* citiraj
APA 6th Edition
Budisa, N. i Pifat, G. (1998). Probing Protein Stability with Non-natural Amino Acids. Croatica Chemica Acta, 71 (1), 179-187. Preuzeto s https://hrcak.srce.hr/132334
MLA 8th Edition
Budisa, Nediljko i Greta Pifat. "Probing Protein Stability with Non-natural Amino Acids." Croatica Chemica Acta, vol. 71, br. 1, 1998, str. 179-187. https://hrcak.srce.hr/132334. Citirano 12.11.2019.
Chicago 17th Edition
Budisa, Nediljko i Greta Pifat. "Probing Protein Stability with Non-natural Amino Acids." Croatica Chemica Acta 71, br. 1 (1998): 179-187. https://hrcak.srce.hr/132334
Harvard
Budisa, N., i Pifat, G. (1998). 'Probing Protein Stability with Non-natural Amino Acids', Croatica Chemica Acta, 71(1), str. 179-187. Preuzeto s: https://hrcak.srce.hr/132334 (Datum pristupa: 12.11.2019.)
Vancouver
Budisa N, Pifat G. Probing Protein Stability with Non-natural Amino Acids. Croatica Chemica Acta [Internet]. 1998 [pristupljeno 12.11.2019.];71(1):179-187. Dostupno na: https://hrcak.srce.hr/132334
IEEE
N. Budisa i G. Pifat, "Probing Protein Stability with Non-natural Amino Acids", Croatica Chemica Acta, vol.71, br. 1, str. 179-187, 1998. [Online]. Dostupno na: https://hrcak.srce.hr/132334. [Citirano: 12.11.2019.]

Sažetak
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

Posjeta: 262 *