## Abstract Unfolding of marginally stable proteins is a significant factor in commercial application of hydrophobic interaction chromatography (HIC). In this work, hydrogen‐deuterium isotope exchange labeling has been used to monitor protein unfolding on HIC media for different stationary phase hy
✦ LIBER ✦
Nucleation mechanism for protein folding and theoretical predictions for hydrogen-exchange labeling experiments
✍ Scribed by D. Thirumalai; Zhuyan Guo
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1995
- Tongue
- English
- Weight
- 402 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0006-3525
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