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NMR h3 JNC’ Couplings Provide Comprehensive Geometrical Constraints for Protein H-bonds in Solution

Nenad Juranić
Martin C. Moncrieffe
Elena Atanasova
Slobodan Macura
Franklyn G. Prendergast

Puni tekst: engleski, pdf (200 KB) str. 503-507 preuzimanja: 523* citiraj
APA 6th Edition
Juranić, N., Moncrieffe, M.C., Atanasova, E., Macura, S. i Prendergast, F.G. (2006). NMR h3 JNC’ Couplings Provide Comprehensive Geometrical Constraints for Protein H-bonds in Solution. Croatica Chemica Acta, 79 (3), 503-507. Preuzeto s https://hrcak.srce.hr/5666
MLA 8th Edition
Juranić, Nenad, et al. "NMR h3 JNC’ Couplings Provide Comprehensive Geometrical Constraints for Protein H-bonds in Solution." Croatica Chemica Acta, vol. 79, br. 3, 2006, str. 503-507. https://hrcak.srce.hr/5666. Citirano 07.03.2021.
Chicago 17th Edition
Juranić, Nenad, Martin C. Moncrieffe, Elena Atanasova, Slobodan Macura i Franklyn G. Prendergast. "NMR h3 JNC’ Couplings Provide Comprehensive Geometrical Constraints for Protein H-bonds in Solution." Croatica Chemica Acta 79, br. 3 (2006): 503-507. https://hrcak.srce.hr/5666
Harvard
Juranić, N., et al. (2006). 'NMR h3 JNC’ Couplings Provide Comprehensive Geometrical Constraints for Protein H-bonds in Solution', Croatica Chemica Acta, 79(3), str. 503-507. Preuzeto s: https://hrcak.srce.hr/5666 (Datum pristupa: 07.03.2021.)
Vancouver
Juranić N, Moncrieffe MC, Atanasova E, Macura S, Prendergast FG. NMR h3 JNC’ Couplings Provide Comprehensive Geometrical Constraints for Protein H-bonds in Solution. Croatica Chemica Acta [Internet]. 2006 [pristupljeno 07.03.2021.];79(3):503-507. Dostupno na: https://hrcak.srce.hr/5666
IEEE
N. Juranić, M.C. Moncrieffe, E. Atanasova, S. Macura i F.G. Prendergast, "NMR h3 JNC’ Couplings Provide Comprehensive Geometrical Constraints for Protein H-bonds in Solution", Croatica Chemica Acta, vol.79, br. 3, str. 503-507, 2006. [Online]. Dostupno na: https://hrcak.srce.hr/5666. [Citirano: 07.03.2021.]

Sažetak
Protein backbone H-bonds (>N–H···O–C<) show relationships between NMR h3JNC' couplings measured in solution and H-bond geometry parameters seen in X-ray crystal structures. Assuming that the solution and crystal structure of protein backbone is the same, the h3JNC' couplings can be calibrated to provide good estimates of both angular and radial H-bond parameters in a solution. The crucial premise of equality between the solution and the crystal structure of protein backbone we validated on the level of the NH-bonds orientation, by comparing the orientations inferred from X-ray crystal structures with the solution ones determined from NMR residual dipolar couplings.

Ključne riječi
hydrogen bonding; proteins; NMR; spin-spin couplings; H-bond geometry

Hrčak ID: 5666

URI
https://hrcak.srce.hr/5666

Posjeta: 798 *