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

Autor: 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.

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 multidimension

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dd4c1084581e9299ab6292947c1a8726
https://europepmc.org/articles/PMC2143925/

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Conformation and orientation of the gene 9 minor coat protein of bacteriophage M13 in phospholipid bilayers.

Autor: Houbiers MC; Department of Biomolecular Sciences, Laboratory of Molecular Physics, Wageningen University and Research Center, Dreijenlaan 3 6703 HA Wageningen, The Netherlands. chantal.houbiers@virus.mf.wau.nl, Wolfs CJ, Spruijt RB, Bollen YJ, Hemminga MA, Goormaghtigh E

Publikováno v: Biochimica et biophysica acta [Biochim Biophys Acta] 2001 Apr 02; Vol. 1511 (2), pp. 224-35.