Characterization of the unfolded state of bovine alpha-lactalbumin and comparison with unfolded states of homologous proteins.
The unfolded states of three homologous proteins with a very similar fold have been investigated by heteronuclear NMR spectroscopy. Secondary structure propensities as derived from interpretation of chemical shifts and motional restrictions as evidenced by heteronuclear (15)N relaxation rates have b...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2006
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