Equilibrium folding studies of cellular retinoic acid binding protein, a predominantly β-sheet protein

Zhi-Ping Liu, Jose Rizo-Rey, Lila M. Gierasch

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Abstract

We have examined the conformational behavior under various unfolding conditions of a predominantly β-sheet protein, cellular retinoic acid binding protein (CRABP). Urea unfolding-refolding of CRABP is a highly cooperative process that can be approximated by a two-state model. Acid denaturation is also cooperative and reversible and leads to a state containing nonnative residual structure: Below pH 2.6, CRABP contains a substantially larger amount of α-helix than under native conditions. CRABP adopts up to 75% α-helix in solutions containing a high percentage of 2,2,2-trifluoroethanol. The acid-denatured state of CRABP undergoes a conformational change to a state containing predominantly β-sheet structure upon the addition of small amounts of Na2SO4. This conformational malleability may be important for the folding mechanism of CRABP. The possible implication of nonnative α-helical structure in the folding of CRABP is discussed.

Original languageEnglish (US)
Pages (from-to)134-142
Number of pages9
JournalBiochemistry
Volume33
Issue number1
StatePublished - 1994

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Retinoic Acid Receptors
Proteins
Trifluoroethanol
Denaturation
Acids
Urea

ASJC Scopus subject areas

  • Biochemistry

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Equilibrium folding studies of cellular retinoic acid binding protein, a predominantly β-sheet protein. / Liu, Zhi-Ping; Rizo-Rey, Jose; Gierasch, Lila M.

In: Biochemistry, Vol. 33, No. 1, 1994, p. 134-142.

Research output: Contribution to journalArticle

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