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Helix Propensities of Amino Acid Residues via Thioester Exchange
We describe the use of thioester exchange equilibria to measure the propensities of amino acid residues to participate in helical secondary structure at room temperature in the absence of denaturants. Thermally or chemically induced unfolding has previously been employed to measure α-helix propensit...
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| Gepubliceerd in: | J Am Chem Soc |
|---|---|
| Hoofdauteurs: | , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
2017
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5995559/ https://ncbi.nlm.nih.gov/pubmed/28898059 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jacs.7b07930 |
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