Direct observation of fast protein folding: the initial collapse of apomyoglobin.

The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the protein-folding history in a single sweep in standard aqueous buffers. The earliest steps during folding to a compact state...

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Detaylı Bibliyografya
Asıl Yazarlar: Ballew, R M, Sabelko, J, Gruebele, M
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 1996
Konular:
Research Article
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC39134/
https://ncbi.nlm.nih.gov/pubmed/8650166
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