Two-state transition between molten globule and unfolded states of acetylcholinesterase as monitored by electron paramagnetic resonance spectroscopy.


Abstract

Cys-231 of Torpedo californica acetylcholinesterase (EC 3.1.1.7) was selectively labeled with the mercury derivative of a stable nitroxyl radical. In 1.5 M guanidinium chloride, this conjugate exists in a molten globule state (MG), whereas in 5 M denaturant, it is in an unfolded state (U). The transition between the two states is reversible. In the MG, the label is highly immobilized, whereas in the U, it is almost freely rotating. The clearly distinct electron paramagnetic resonance (EPR) spectra of the two states permits the study of this transition. Upon elevating the guanidinium chloride concentration, a decrease in the EPR signal of the MG occurs concomitantly with an increase in the U signal, the total intensity of the EPR spectra remaining constant. This behavior is characteristic of a two-state transition. The thermodynamic characteristics of this transition (delta G0 and m), whether estimated directly from the EPR data or from both CD and fluorescence data analyzed by assuming a two-state scheme, are in good agreement. Study holds ProTherm entries: 10584, 10585, 10586 Extra Details: molten globule state; electron paramagnetic resonance; two-state transition

Submission Details

ID: qkjAzXmS

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:40 p.m.

Version: 1

Publication Details
Kreimer DI;Szosenfogel R;Goldfarb D;Silman I;Weiner L,Proc. Natl. Acad. Sci. U.S.A. (1994) Two-state transition between molten globule and unfolded states of acetylcholinesterase as monitored by electron paramagnetic resonance spectroscopy. PMID:7991597
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1ACJ 1993-08-18T00:00:00+0000 2.8 QUATERNARY LIGAND BINDING TO AROMATIC RESIDUES IN THE ACTIVE-SITE GORGE OF ACETYLCHOLINESTERASE
1ACL 1993-08-18T00:00:00+0000 2.8 QUATERNARY LIGAND BINDING TO AROMATIC RESIDUES IN THE ACTIVE-SITE GORGE OF ACETYLCHOLINESTERASE
1AMN 1996-02-13T00:00:00+0000 2.8 TRANSITION STATE ANALOG: ACETYLCHOLINESTERASE COMPLEXED WITH M-(N,N,N-TRIMETHYLAMMONIO)TRIFLUOROACETOPHENONE
1AX9 1997-11-03T00:00:00+0000 2.8 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, LAUE DATA
1CFJ 1999-03-19T00:00:00+0000 2.6 METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED) OBTAINED BY REACTION WITH O-ISOPROPYLMETHYLPHOSPHONOFLUORIDATE (GB, SARIN)
1DX6 1999-12-21T00:00:00+0000 2.3 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-GALANTHAMINE AT 2.3A RESOLUTION
1E3Q 2000-06-21T00:00:00+0000 2.85 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH BW284C51
1E66 2000-08-08T00:00:00+0000 2.1 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-HUPRINE X AT 2.1A RESOLUTION
1EA5 2000-11-06T00:00:00+0000 1.8 NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO CALIFORNICA at 1.8A resolution
1EEA 1999-01-26T00:00:00+0000 4.5 Acetylcholinesterase

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
97.6 Acetylcholinesterase P07692 ACES_TORMA
100.0 Acetylcholinesterase P04058 ACES_TETCF