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1 H and 15 N chemical shift assignments of a carboxy‐terminal functional domain of the bacteriophage P22 scaffolding protein
Author(s) -
Sun Yahong,
Rama Krish.
Publication year - 1999
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/(sici)1097-458x(199908)37:8<602::aid-mrc505>3.0.co;2-x
Subject(s) - chemistry , terminal (telecommunication) , bacteriophage , chemical shift , helix (gastropod) , stereochemistry , biochemistry , gene , escherichia coli , telecommunications , computer science , ecology , biology , snail
The 15 N‐labeled C ‐terminal functional domain of the bacteriophage P22 scaffolding protein was expressed and purified. The NMR chemical‐shift assignments of this functional domain were determined. An analysis of the chemical shift indices for the α‐protons indicates that the N ‐terminal half of this protein is unstructured whereas the C‐terminal half is defined by a helix–loop–helix motif. Copyright © 1999 John Wiley & Sons, Ltd.