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Folding of protein fragments: Conformational and biological studies on thioredoxin and its fragments

✍ Scribed by Herbert Reutimann; Pier Luigi Luisi; Arne Holmgren

Publisher: Wiley (John Wiley & Sons)
Year: 1983
Tongue: English
Weight: 291 KB
Volume: 22
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360220117

No coin nor oath required. For personal study only.

✦ Synopsis

Thioredoxin can be cleaved enzymatically into the two fragments (1-73) and (74-108) and chemically into two different ones (1-37) and . In this paper, the conformational properties of the short fragment (1-37) are reported and compared with those of the larger fragment (1-73). Using mainly circular dichroism (CD), it is shown that the (1-37) fragment, which contains the active disulfide unit center, is present as an unordered structure in the neutral pH range, but assumes a rigid folding at pH values below 6. The form of the CD spectrum is very similar to that of the complete native protein, and to that of the folded (1-73) fragment. The possible mechanisms for refolding of the short fragment are discussed.

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