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Folding of protein fragments: Conformational and biological studies on thioredoxin and its fragments
Author(s) -
Reutimann Herbert,
Luisi Pier Luigi,
Holmgren Arne
Publication year - 1983
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360220117
Subject(s) - chemistry , fragment (logic) , circular dichroism , folding (dsp implementation) , disulfide bond , protein folding , crystallography , stereochemistry , thioredoxin , biochemistry , enzyme , programming language , computer science , electrical engineering , engineering
Thioredoxin can be cleaved enzymatically into the two fragments (1–73) and (74–108) and chemically into two different ones (1–37) and (38–108). 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.