Reversible disulfide bond formation of intracellular proteins probed by NMR spectroscopy
✍ Scribed by Kirill Piotukh; Daniela Kosslick; Jürgen Zimmermann; Eberhard Krause; Christian Freund
- Book ID
- 113630373
- Publisher
- Elsevier Science
- Year
- 2007
- Tongue
- English
- Weight
- 674 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0891-5849
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📜 SIMILAR VOLUMES
The feasibility of using diusion-ordered NMR spectroscopy (DOSY) as a useful probe to qualitatively understand the relative strength of hydrogen bonds between various components in a mixture and a ligand in non-aqueous solutions has been demonstrated. 1 H-detected DOSY and 31 P-detected DOSY were us
It is well established that the oxidation state of cysteine residues in proteins is critical to overall physical stability. Disulfide bonds most often impart thermodynamic stability, but in some cases, diminish it. Predicting the circumstances that lead to each outcome is difficult because mechanist