Initial hydrophobic collapse in the folding of barstar
Article Abstract:
A study of the initial hydrophobic collapse in the folding of barstar, a small protein, reveals that the polypeptide chain undergoes a fast collapse to a compact globule. This packed globule contains a hydrophobic core that is solvent-accessible, but incorporates no optically active secondary or tertiary structure. Furthermore, the data shows that the formation of a compact but structureless globule by nonspecific hydrophobic collapse is preceded by the formation of the molten, globule-like intermediate on the folding pathway.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Betas are brought into the fold
Article Abstract:
Researchers led by Samuel Gellman and Dieter Seebach have discovered that chains of six beta-amino-acid units can fold into well-defined helices in methanol solution. Using trans-2-aminocyclohexanecarboxylic acid, the folding pattern yielded 14-atom 'rings' formed by hydrogen bonds. Aside from broadening molecular engineers' realm, this finding suggests that links of naturally occurring alpha-amino acids do not monopolize folded structures.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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