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Apoflavodoxin (un)folding followed at the residue level by NMR.

The denaturant-induced (un)folding of apoflavodoxin from Azotobacter vinelandii has been followed at the residue level by NMR spectroscopy. NH groups of 21 residues of the protein could be followed in a series of 1H-15N heteronuclear single-quantum coherence spectra recorded at increasing concentrat...

詳細記述

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書誌詳細
主要な著者: van Mierlo, C. P., van den Oever, J. M., Steensma, E.
フォーマット: Artigo
言語:Inglês
出版事項: Cold Spring Harbor Laboratory Press 2000
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC2144449/
https://ncbi.nlm.nih.gov/pubmed/10739257
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