Multi-conformational peptide dynamics derived from NMR data: A new search algorithm and its application to antamanide
| Autor: | M. J. Blackledge, Rafael Brüschweiler, Richard R. Ernst |
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| Rok vydání: | 1991 |
| Předmět: |
Models
Molecular chemistry.chemical_classification Magnetic Resonance Spectroscopy Biomolecule Molecular Sequence Data Scalar (mathematics) Relaxation (NMR) Molecular Conformation Biomolecular structure Peptides Cyclic Biochemistry Molecular dynamics chemistry.chemical_compound chemistry Antamanide Search algorithm Computational chemistry Amino Acid Sequence Peptides Two-dimensional nuclear magnetic resonance spectroscopy Algorithms Spectroscopy |
| Zdroj: | Journal of Biomolecular NMR. 1:3-11 |
| ISSN: | 1573-5001 0925-2738 |
| DOI: | 10.1007/bf01874565 |
| Popis: | A search algorithm, called MEDUSA, is presented which allows the determination of multiple conformations of biomolecules in solution with exchange rate constants typically between 10(3) and 10(7) s-1 on the basis of experimental high-resolution NMR data. Multiples of structures are generated which are consistent as ensembles with NMR cross-relaxation rates (NOESY, ROESY), scalar J-coupling constants, and T1 rho measurements. The algorithm is applied to the cyclic decapeptide antamanide dissolved in chloroform. The characteristic radio-frequency field dependence of the T1 rho relaxation rates found for the NH protons of Val1 and Phe6 can be explained by a dynamical exchange between two structures. |
| Databáze: | OpenAIRE |
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