Response of native and denatured hen lysozyme to high pressure studied by (15)N/(1)H NMR spectroscopy.
High-pressure (15)N/(1)H NMR techniques were used to characterize the conformational fluctuations of hen lysozyme, in its native state and when denatured in 8 M urea, over the pressure range 30--2000 bar. Most (1)H and (15)N signals of native lysozyme show reversible shifts to low field with increas...
প্রধান লেখক: | Kamatari, Y, Yamada, H, Akasaka, K, Jones, J, Dobson, C, Smith, L |
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বিন্যাস: | Journal article |
ভাষা: | English |
প্রকাশিত: |
2001
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অনুরূপ উপাদানগুলি
অনুরূপ উপাদানগুলি
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Conformational fluctuations of hen lysozyme investigated by high pressure NMR spectroscopy
অনুযায়ী: Kamatari, Y, অন্যান্য
প্রকাশিত: (2003) -
Cavity hydration as a gateway to unfolding: an NMR study of hen lysozyme at high pressure and low temperature.
অনুযায়ী: Kamatari, Y, অন্যান্য
প্রকাশিত: (2011) -
Side-chain conformations in an unfolded protein: chi1 distributions in denatured hen lysozyme determined by heteronuclear 13C, 15N NMR spectroscopy.
অনুযায়ী: Hennig, M, অন্যান্য
প্রকাশিত: (1999) -
Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques.
অনুযায়ী: Wilkins, D, অন্যান্য
প্রকাশিত: (1999) -
Antibacterial Activity of Hen Egg White Lysozyme Denatured by Thermal and Chemical Treatments
অনুযায়ী: Rubén Vilcacundo, অন্যান্য
প্রকাশিত: (2018-10-01)