期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 135, 期 28, 页码 10278-10281出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja404677c
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资金
- NSF
- DOE
- Danish Council for Independent Research \ Natural Sciences
- National Institutes of Health [RR022200]
- NSF [TG-MCB070039]
- NATIONAL CENTER FOR RESEARCH RESOURCES [R01RR022200] Funding Source: NIH RePORTER
Peptide TZ1C2 can populate two distinct orientations: a staggered (out-of-register) fibril and an aligned (in-register) coiled-coil trimer. The coordination of two cadmium ions induces a registry shift that results in a reversible transition between these structural forms. This process recapitulates the self-assembly mechanism of native protein fibrils in which a ligand binding event gates a reversible conformational transition between alternate forms of a folded peptide structure.
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