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Conformational intermediates in the folding of a coiled-coil model peptide of the N-terminus of tropomyosin and alpha alpha-tropomyosin.

Circular dichroism was used to study the folding of alpha alpha-tropomyosin and AcTM43, a 43-residue peptide designed to serve as a model for the N-terminal domain of tropomyosin. The sequence of the peptide is AcMDAIKKKMQMLKLDVENLLDRLEQLEADLKALEDRYKQLEGGC. The peptide appeared to form a coiled coil...

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Detaylı Bibliyografya
Asıl Yazarlar: Greenfield, N. J., Hitchcock-DeGregori, S. E.
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Cold Spring Harbor Laboratory Press 1993
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC2142446/
https://ncbi.nlm.nih.gov/pubmed/8401212
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