NDLI: Two partially unfolded states of Torpedo californica acetylcholinesterase.

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Two partially unfolded states of Torpedo californica acetylcholinesterase.

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Two partially unfolded states of Torpedo californica acetylcholinesterase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kreimer, D. I. Shin, I. Weiner, L. Silman, I. Shnyrov, V. L. Villar, E.
Description	Country affiliation: Israel Author Affiliation: Kreimer DI ( Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel.)
Abstract	Chemical modification with sulfhydryl reagents of the single, nonconserved cysteine residue Cys231 in each subunit of a disulfide-linked dimer of Torpedo californica acetylcholinesterase produces a partially unfolded inactive state. Another partially unfolded state can be obtained by exposure of the enzyme to 1-2 M guanidine hydrochloride. Both these states display several important features of a molten globule, but differ in their spectroscopic (CD, intrinsic fluorescence) and hydrodynamic (Stokes radii) characteristics. With reversal of chemical modification of the former state or removal of denaturant from the latter, both states retain their physiochemical characteristics. Thus, acetylcholinesterase can exist in two molten globule states, both of which are long-lived under physiologic conditions without aggregating, and without either intraconverting or reverting to the native state. Both states undergo spontaneous intramolecular thioldisulfide exchange, implying that they are flexible. As revealed by differential scanning calorimetry, the state produced by chemical modification lacks any heat capacity peak, presumably due to aggregation during scanning, whereas the state produced by guanidine hydrochloride unfolds as a single cooperative unit, thermal transition being completely reversible. Sucrose gradient centrifugation reveals that reduction of the interchain disulfide of the native acetylcholinesterase dimer converts it to monomers, whereas, after such reduction, the two subunits remain completely associated in the partially unfolded state generated by guanidine hydrochloride, and partially associated in that produced by chemical modification. It is suggested that a novel hydrophobic core, generated across the subunit interfaces, is responsible for this noncovalent association. Transition from the unfolded state generated by chemical modification to that produced by guanidine hydrochloride is observed only in the presence of the denaturant, yielding, on extrapolation to zero guanidine hydrochloride, a high free energy barrier (ca. 23.8 kcal/mol) separating these two flexible, partially unfolded states.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	5
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1996-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acetylcholinesterase Chemistry Protein Folding Torpedo Animals Calorimetry, Differential Scanning Chemical Phenomena Chemistry, Physical Cholinesterase Inhibitors Pharmacology Circular Dichroism Cysteine Disulfides Dithiothreitol Electric Organ Enzymology Electron Spin Resonance Spectroscopy Guanidine Guanidines Macromolecular Substances Spectrometry, Fluorescence Sulfhydryl Reagents Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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