Solvent Exchange Rates of Side-chain Amide Protons in Proteins
β Scribed by Ponni Rajagopal; Bryan E. Jones; Rachel E. Klevit
- Book ID
- 110261466
- Publisher
- Springer Netherlands
- Year
- 1998
- Tongue
- English
- Weight
- 178 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0925-2738
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It has long been recognized that stereospecific reso-angles in asparagine and glutamine side chains, respectively, and it may not always be obvious which resonance nance assignments significantly improve the quality of protein structures determined by NMR ( 1 -8 ) . Both the belongs to which positio
We have used a modified version of a previously proposed technique, MEXICO [Gemmecker et al. (1993) J. Am. Chem. Soc., 115, 11620], and improved data analysis procedures in order to measure rapid hydrogen exchange (HX) rates of amide protons in peptides labeled only with 15N. The requirement of 13C-