Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR
Copyright 2004 John Wiley & Sons, Ltd.
| Veröffentlicht in: | Magnetic resonance in chemistry : MRC. - 1985. - 42(2004), 2 vom: 15. Feb., Seite 267-75 |
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| Weitere Verfasser: | , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2004
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| Zugriff auf das übergeordnete Werk: | Magnetic resonance in chemistry : MRC |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Carbon Isotopes Peptide Fragments Peptides Polylysine 25104-18-1 Hydrogen 7YNJ3PO35Z mehr... |
| Zusammenfassung: | Copyright 2004 John Wiley & Sons, Ltd. Elastin is the main structural protein that provides elasticity to various tissues and organs in vertebrates. Molecular motions are believed to play a significant role in its elasticity. We have used solid-state NMR spectroscopy to characterize the dynamics of an elastin-mimetic protein as a function of hydration to better understand the origin of elastin elasticity. Poly(Lys-25), [(VPGVG)(4)(VPGKG)](39), has a repeat sequence common to natural elastin. (13)C cross-polarization and direct polarization spectra at various hydration levels indicate that water enhances the protein motion in a non-uniform manner. Below 20% hydration, the backbone motion increases only slightly whereas above 30% hydration, both the backbone and the side-chains undergo large-amplitude motions. The motional amplitudes are extracted from (13)C-(1)H and (1)H-(1)H dipolar couplings using 2D isotropic-anisotropic correlation experiments. The root mean square fluctuation angles are found to be 11-18 degrees in the dry protein and 16-21 degrees in the 20% hydrated protein. Dramatically, the amplitudes increase to near isotropic at 30% hydration. Field-dependent (1)H rotating-frame spin-lattice relaxation times (T(1rho)) indicate that significant motions occur on the microsecond time-scale (1.2-2.3 micros). The large-amplitude and low-frequency motion of poly(Lys-25) at relatively mild hydration indicates that the conformational entropy of the protein in the relaxed state contributes significantly to the elasticity |
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| Beschreibung: | Date Completed 22.03.2005 Date Revised 21.11.2013 published: Print Citation Status MEDLINE |
| ISSN: | 1097-458X |