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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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Detaylı Bibliyografya
Asıl Yazarlar: Gilmanshin, R., Dyer, R. B., Callender, R. H.
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Cold Spring Harbor Laboratory Press 1997
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143565/
https://ncbi.nlm.nih.gov/pubmed/9336836
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