β-Sheet folding mechanisms from perturbation energetics
✍ Scribed by Songpon Deechongkit; Houbi Nguyen; Marcus Jager; Evan T Powers; Martin Gruebele; Jeffery W Kelly
- Book ID
- 113883054
- Publisher
- Elsevier Science
- Year
- 2006
- Tongue
- English
- Weight
- 462 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0959-440X
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The folding mechanism of cellular retinoic acid binding protein I (CRABP I), cellular retinol binding protein II (CRBP II), and intestinal fatty acid binding protein (IFABP) were investigated to determine if proteins with similar native structures have similar folding mechanisms. These mostly -shee
## Abstract We had earlier observed that the detailed nature of the β‐structure adopted by poly(L‐tyrosine) depends on molecular weight [Auer, H. E. & McKnight, R. P. (1978) __Biochemistry__ **17**, 2798–2805]. It was proposed that shorter molecules form an open, single‐layered sheet (class I) and