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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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| Hlavní autoři: | , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Cold Spring Harbor Laboratory Press
2006
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| Témata: | |
| On-line přístup: | 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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