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Disulfide crosslinks to probe the structure and flexibility of a designed four-helix bundle protein.
The introduction of disulfide crosslinks is a generally useful method by which to identify regions of a protein that are close together in space. Here we describe the use of disulfide crosslinks to investigate the structure and flexibility of a family of designed 4-helix bundle proteins. The results...
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| Hoofdauteurs: | , , , |
|---|---|
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Cold Spring Harbor Laboratory Press
1994
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2142780/ https://ncbi.nlm.nih.gov/pubmed/7756995 |
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