Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 22, Pages 18201-18209Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.285163
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Funding
- National Science Foundation [MCB-0344975, MCB-1022526]
- Australian Research Council
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1022526] Funding Source: National Science Foundation
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In this study, one- and two-dimensional NMR experiments are applied to uniformly N-15-enriched synthetic elastin, a recombinant human tropoelastin that has been cross-linked to form an elastic hydrogel. Hydrated elastin is characterized by large segments that undergo liquid-like motions that limit the efficiency of cross-polarization. The refocused insensitive nuclei enhanced by polarization transfer experiment is used to target these extensive, mobile regions of this protein. Numerous peaks are detected in the backbone amide region of the protein, and their chemical shifts indicate the completely unstructured, random coil model for elastin is unlikely. Instead, more evidence is gathered that supports a characteristic ensemble of conformations in this rubber-like protein.
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