Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR
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چکیده
منابع مشابه
Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR
The structures of apomyoglobin folding intermediates have been widely analyzed using physical chemistry methods including fluorescence, circular dichroism, small angle X-ray scattering, NMR, mass spectrometry, and rapid mixing. So far, at least two intermediates (on sub-millisecond- and millisecond-scales) have been demonstrated for apomyoglobin folding. The combination of pH-pulse labeling and...
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Sph site of pSL301 (Invitrogen). Colonies were screened for inserts by PCR with T7 and T3 sequences located outside the cloning site as primers. 10. Selected clones were manually sequenced as described [G. (1989)] with 5'-GACGTCGAC-CTGAGGTAATTATAACC-3' as primer. Sequence files were analyzed by means of the SAGE software group (7), which identifies the anchoring enzyme site with the proper spac...
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ژورنال
عنوان ژورنال: Proceedings of the Japan Academy, Series B
سال: 2017
ISSN: 0386-2208,1349-2896
DOI: 10.2183/pjab.93.002