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Characterization of the unfolded state of bovine α-lactalbumin and comparison with unfolded states of homologous proteins
The unfolded states of three homologous proteins with a very similar fold have been investigated by heteronuclear NMR spectroscopy. Secondary structure propensities as derived from interpretation of chemical shifts and motional restrictions as evidenced by heteronuclear (15)N relaxation rates have b...
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| 主要な著者: | , , , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Cold Spring Harbor Laboratory Press
2006
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2242548/ https://ncbi.nlm.nih.gov/pubmed/16731974 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.051974506 |
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