Comparative Carbon-13 Nuclear Magnetic Resonance Study at 67.9 MHz on Lysozyme (Human and Egg-White) and α-Lactalbumin (Human and Bovine) in Their Native and Denatured State
✍ Scribed by Georges Van Binst; Monique Biesemans; A. O. Barel
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2010
- Weight
- 297 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0037-9646
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✦ Synopsis
Abstract
A first detailed comparison of the ^13^C spectra at high field of two lysozymes (human and egg‐white) and two α‐lactalbumins (human and bovine milk) is presented. Assignments were made on most of the resonance peaks in the aliphatic and aromatic regions of the denatured proteins. The relative peak intensities clearly demonstrate the differences in the amino acid composition of the related proteins. The broadening and the complexity of the spectra of the native proteins reflect the non equivalence of the chemical groups in the folded conformation. The usefulness of ^13^C nmr spectroscopy in the study of the interaction between small molecules and proteins was tested on N‐acetylglucosamine in the presence of lysozyme.