Assignment of the 13C-nmr spectra of virgin and reactive-site modified turkey ovomucoid third domain
β Scribed by A. D. Robertson; G. I. Rhyu; W. M. Westler; J. L. Markley
- Book ID
- 101719722
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1990
- Tongue
- English
- Weight
- 455 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
The virgin (reactive-site Leu'8-Glu'9 peptide bond intact) and modified (reactive-site Leu'X-Glu'9 peptide bond hydrolyzed) forms of turkey ovomucoid third domain (OMTKY3 and OMTKY3*, respectively) have been analyzed by proton-detected 'H{I3C} twodimensional single-bond correlation (1H{13C}SBC) spectroscopy. Previous 'H-nmr assignments of these proteins [A
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## Abstract The substrateβlike inhibition of serine proteinases by avian ovomucoid domains has provided an excellent model for protein inhibitorβproteinase interactions of the standard type. ^1^H,^15^N and ^13^C NMR studies have been undertaken on complexes formed between turkey ovomucoid third dom
## Abstract P14C/N39C is the disulfide variant of the ovomucoid third domain from silver pheasant (OMSVP3) introducing an engineered Cys^14^ο£ΏCys^39^ bond near the reactive site on the basis of the sequence homology between OMSVP3 and ascidian trypsin inhibitor. This variant exhibits a narrower inhi