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Folding Mechanism of Three Structurally Similar β-Sheet Proteins by Lora L. Burns; Paula M. Dalessio; Ira J. Ropson is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The folding mechanism of cellular retinoic acid binding protein I (CRABP I), cellular retinol binding protein II (CRBP II), and intestinal fatty acid binding protein (IFABP) were investigated to determine if proteins with similar native structures have similar folding mechanisms. These mostly ␤-sheet proteins have very similar structures, despite having as little as 33% sequence similarity. The reversible urea denaturation of these proteins was characterized at equilibrium by circular dichroism and fluorescence. The data were best fit by a two-state model for each of these proteins, suggesting that no significant population of folding intermediates were present at equilibrium. The native states were of similar stability with free energies (linearly extrapolated to 0 M urea, ⌬G H 2 O ) of 6.5, 8.3, and 5.5 kcal/mole for CRABP I, CRBP II, and IFABP, respectively. The kinetics of the folding and unfolding processes for these proteins was monitored by stopped-flow CD and fluorescence. Intermediates were observed during both the folding and unfolding of all of these proteins. However, the overall rates of folding and unfolding differed by nearly three orders of magnitude. Further, the s

Who reads Folding Mechanism of Three Structurally Similar β-Sheet Proteins?

Author

Lora L. Burns; Paula M. Dalessio; Ira J. Ropson

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

1998

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)