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A cross-strand Trp–Trp pair stabilizes the hPin1 WW domain at the expense of function
Using the human Pin1 WW domain (hPin1 WW), we show that replacement of two nearest neighbor non-hydrogen-bonded residues on adjacent β-strands with tryptophan (Trp) residues increases β-sheet thermodynamic stability by 4.8 kJ mol(−1) at physiological temperature. One-dimensional NMR studies confirme...
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| Hlavní autoři: | , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Cold Spring Harbor Laboratory Press
2007
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2204138/ https://ncbi.nlm.nih.gov/pubmed/17766376 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.072904107 |
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