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Structural heterogeneity of the various forms of apomyoglobin: implications for protein folding.
Temperature-induced denaturation transitions of different structural forms of apomyoglobin were studied monitoring intrinsic tryptophan fluorescence. It was found that the tryptophans are effectively screened from solvent both in native and acid forms throughout most of the temperature range tested....
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| Asıl Yazarlar: | , , |
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| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
Cold Spring Harbor Laboratory Press
1997
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2143565/ https://ncbi.nlm.nih.gov/pubmed/9336836 |
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