期刊
CHEMICAL COMMUNICATIONS
卷 53, 期 23, 页码 3319-3322出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7cc00307b
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资金
- ERC Marie Curie Early Career Development Grant
- European Commission
- Swedish Research Council
- Swedish Research Council [2014-10371, 2014-2408]
- Center for Innovative Medicine (CIMED) at Karolinska Institutet
- Stockholm City Council
- ERC Advanced Investigator Award ENABLE [641317]
- Welcome Trust Investigator Award [104633/Z/14/Z]
- Medical Research Council Program Grant [MR/N020413/1]
- FORMAS [942-2015-629]
- MRC [MR/N020413/1] Funding Source: UKRI
- Wellcome Trust [104633/Z/14/Z] Funding Source: Wellcome Trust
- Medical Research Council [MR/N020413/1] Funding Source: researchfish
- Wellcome Trust [104633/Z/14/Z] Funding Source: researchfish
Self-assembling proteins, the basis for a broad range of biological scaffolds, are challenging to study using most structural biology approaches. Here we show that mass spectrometry (MS) in combination with MD simulations captures structural features of short-lived oligomeric intermediates in spider silk formation, providing direct insights into its complex assembly process.
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