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.

Polypeptides

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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.

Analysis, Molecular structure, Branched chain amino acids

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