NMR-based localization of ions involved in salting out of hen egg white lysozyme. | Zendy

Jarosław Poznański | Zendy

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NMR-based localization of ions involved in salting out of hen egg white lysozyme.

Author(s) -

Jarosław Poznański

Publication year - 2006

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2006_3357

Subject(s) - lysozyme , chemistry , salting out , salting , salt (chemistry) , egg white , ion , sodium , nuclear magnetic resonance spectroscopy , crystallography , chemical shift , biochemistry , stereochemistry , aqueous solution , organic chemistry , food science

NaCl-induced aggregation of hen egg white lysozyme (HEWL) was monitored by NMR spectroscopy. Small, but significant, changes induced by salt addition in TOCSY spectra were attributed to the effect of local reorganization of protein backbone upon ion binding. Salt-induced variations in HN and H alpha chemical shifts were mapped on the HEWL 3D structure which allowed the construction of a scheme of the spatial localization of potential ion binding sites. It was found that in a 0.5 M NaCl solution six chloride anions and at least one sodium cation are bound to preferred sites on the HEWL surface.

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