Document Detail

Equilibrium denaturation studies of mouse beta-nerve growth factor.
MedLine Citation:
PMID:  1304906     Owner:  NLM     Status:  MEDLINE    
Equilibrium denaturation of dimeric mouse beta-nerve growth factor (beta-NGF) has been studied by monitoring changes in the protein's spectroscopic characteristics. Denaturation of beta-NGF in guanidine hydrochloride and urea resulted in an altered intrinsic fluorescence emission spectrum, fluorescence depolarization, and diminished negative circular dichroism. Native-like spectroscopic properties and specific biological activity are restored when denaturant is diluted from unfolded samples, demonstrating that this process is fully reversible. However, refolding of denatured beta-NGF is dependent on the three disulfide bonds present in the native protein and does not readily occur when the disulfide bonds are reduced. Graphical analysis and nonlinear least-squares fitting of beta-NGF denaturation data demonstrate that denaturation is dependent on the concentration of beta-NGF and is consistent with a two-state model involving native dimer and denatured monomer (N2 = 2D). The conformational stability of mouse beta-NGF calculated according to this model is 19.3 +/- 1.1 kcal/mol in 100 mM sodium phosphate at pH 7. Increasing the hydrogen ion concentration resulted in a 25% decrease in beta-NGF stability at pH 4 relative to pH 7.
D E Timm; K E Neet
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Protein science : a publication of the Protein Society     Volume:  1     ISSN:  0961-8368     ISO Abbreviation:  Protein Sci.     Publication Date:  1992 Feb 
Date Detail:
Created Date:  1993-07-09     Completed Date:  1993-07-09     Revised Date:  2010-09-07    
Medline Journal Info:
Nlm Unique ID:  9211750     Medline TA:  Protein Sci     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  236-44     Citation Subset:  IM    
Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106.
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MeSH Terms
Circular Dichroism
Dose-Response Relationship, Drug
Guanidines / pharmacology
Hydrogen-Ion Concentration
Nerve Growth Factors / chemistry*,  drug effects
Protein Denaturation*
Protein Folding
Spectrometry, Fluorescence
Ultraviolet Rays
Urea / pharmacology
Grant Support
Reg. No./Substance:
0/Guanidines; 0/Nerve Growth Factors; 113-00-8/Guanidine; 57-13-6/Urea

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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