The interactions of Escherichia coli trp repressor with tryptophan and with an operator oligonucleotide. NMR studies using selectively 15N-labelled protein
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1994.00601.x/fullpdf
Reference32 articles.
1. Sequence-specific proton NMR assignments and secondary structure in solution of Escherichia coli trp repressor
2. Unusual dynamic features of the trp repressor from Escherichia coli
3. The solution structures of Escherichia coli trp repressor and trp aporepressor at an intermediate resolution
4. Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR
5. Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques
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