Comparison of NMR structural and dynamics features of the urea and guanidine-denatured states of GED
β Scribed by Jeetender Chugh; Shilpy Sharma; Ramakrishna V. Hosur
- Book ID
- 116178342
- Publisher
- Elsevier Science
- Year
- 2009
- Tongue
- English
- Weight
- 723 KB
- Volume
- 481
- Category
- Article
- ISSN
- 0003-9861
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The spin-lattice relaxation times (TI) of the 170 nucleus of a water molecule in guanidine hydrochloride, urea, and alkylated ureas at 25 \*C were measured by NMR spectroscopy. Urea has no significant effect on the water structure. Also, guanidine hydrochloride as a stronger denaturant than urea doe
## Abstract The structure and dynamics of the ureaβdenatured B1 immunoglobulin binding domain of streptococcal protein G (GB1) has been investigated by multidimensional heteronuclear NMR spectroscopy. Complete ^1^H, ^15^N, and ^13^C assignments are obtained by means of sequential throughβbond corre