- Abstract:
-
RDCs for the 14 kDa protein hen egg-white lysozyme (HEWL) have been measured in eight different alignment media. The elongated shape and strongly positively charged surface of HEWL appear to limit the protein to four main alignment orientations. Furthermore, low levels of alignment and the protein's interaction with some alignment media increases the experimental error. Together with heterogeneity across the alignment media arising from constraints on temperature, pH and ionic strength for so...
Expand abstract - Publisher copy:
- 10.1007/s10858-010-9457-1
-
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- Journal:
- Journal of Biomolecular NMR
- Volume:
- 49
- Issue:
- 1
- Pages:
- 53-60
- Publication date:
- 2011-01-05
- DOI:
- EISSN:
-
1573-5001
- ISSN:
-
0925-2738
- URN:
-
uuid:84e3a14e-ddae-4c98-b2e8-250772d78174
- Source identifiers:
-
120563
- Local pid:
- pubs:120563
- Language:
- English
- Keywords:
- Copyright date:
- 2011
Journal article
Residual dipolar couplings: Are multiple independent alignments always possible?
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