NDLI: Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway.

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Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Loh, S. N. Baldwin, R. L. Kay, M. S.
Description	Author Affiliation: Loh SN ( Department of Biochemistry, Stanford University Medical Center, CA 94305-5307, USA.);
Abstract	Apomyoglobin folding proceeds through a molten globule intermediate (low-salt form; I1) that has been characterized by equilibrium (pH 4) and kinetic (pH 6) folding experiments. Of the eight alpha-helices in myoglobin, three (A, G, and H) are structured in I1, while the rest appear to be unfolded. Here we report on the structure and stability of a second intermediate, the trichloroacetate form of the molten globule intermediate (I2), which is induced either from the acid-unfolded protein or from I1 by > or = 5 mM sodium trichloroacetate. Circular dichroism measurements monitoring urea- and acid-induced unfolding indicate that I2 is more highly structured and more stable than I1. Although I2 exhibits properties closer to those of the native protein, one-dimensional NMR spectra show that it maintains the lack of fixed side-chain structure that is the hallmark of a molten globule. Amide proton exchange and 1H-15N two-dimensional NMR experiments are used to identify the source of the extra helicity observed in I2. The results reveal that the existing A, G, and H helices present in I1 have become more stable in I2 and that a fourth helix--the B helix--has been incorporated into the molten globule. Available evidence is consistent with I2 being an on-pathway intermediate. The data support the view that apomyoglobin folds in a sequential fashion through a single pathway populated by intermediates of increasing structure and stability.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	12
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Apoproteins Chemistry Myoglobin Protein Folding Metabolism Circular Dichroism Magnetic Resonance Spectroscopy Protein Conformation Thermodynamics Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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