The equilibrium folding pathway of staphylococcal nuclease (SNase) has been approximated using a statistical thermodynamic formalism that utilizes the highresolution structure of the native state as a template to generate a large ensemble of partially folded states. Close to 400,000 different states
β¦ LIBER β¦
Initial Studies of the Equilibrium Folding Pathway of Staphylococcal Nuclease
β Scribed by Wang, Y.; Alexandrescu, A. T.; Shortle, D.
- Book ID
- 120153148
- Publisher
- The Royal Society
- Year
- 1995
- Tongue
- English
- Weight
- 979 KB
- Volume
- 348
- Category
- Article
- ISSN
- 0080-4622
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## Abstract The Nβterminal short fragments of staphylococcal nuclease (SNase), SNase20, SNase28, and SNase36, corresponding to the sequence regions, Ala1βGly20, Ala1βLys28, and Ala1βLeu36, respectively, as well as an 8βresidue peptide (Ala17βIle18βAsp19βGly20βAsp21βThr22βVal23βLys24) have been synt
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