Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding.

As a first step to determine the folding pathway of a protein with an alpha/beta doubly wound topology, the 1H, 13C, and 15N backbone chemical shifts of Azotobacter vinelandii holoflavodoxin II (179 residues) have been determined using multidimensional NMR spectroscopy. Its secondary structure is sh...

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Gorde:
Xehetasun bibliografikoak
Egile Nagusiak: Steensma, E., Nijman, M. J., Bollen, Y. J., de Jager, P. A., van den Berg, W. A., van Dongen, W. M., van Mierlo, C. P.
Formatua: Artigo
Hizkuntza:Inglês
Argitaratua: Cold Spring Harbor Laboratory Press 1998
Gaiak:
Research Article
Sarrera elektronikoa:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143925/
https://ncbi.nlm.nih.gov/pubmed/9521106
Etiketak: Etiketa erantsi
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