EurekaMag.com logo
+ Site Statistics
References:
53,214,146
Abstracts:
29,074,682
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

A partially folded Intermediate during tubulin unfolding: Its detection and spectroscopic characterization



A partially folded Intermediate during tubulin unfolding: Its detection and spectroscopic characterization



Biochemistry 34(21): 6925-6931



The unfolding reaction of the dimeric protein tubulin, isolated from goat brain, was studied using fluorescence and circular dichroism techniques. The unfolding of the tubulin dimer was found to be a two-step process at pH 7. The first step leads to the formation of an intermediate conformation, stable at around 1-2 M urea, followed by a second step that was due to unfolding of the intermediate state. At pH 3, the urea-induced biphasic unfolding profiles obtained at pH 7 became a one-step process indicating that a stable intermediate was also formed at this pH. The intermediate at pH 3 was more stable toward urea denaturation than that at pH 7. The intermediate state has about 60% secondary structure, partially exposed aromatic residues, and less tertiary structure as compared to the native states. Also, hydrophobic surfaces were more exposed in the intermediate than in the native or unfolded states. These results indicate that the intermediate state observed during tubulin unfolding is not only distinct from both the native and unfolded forms but also possesses some properties characteristic of a molten globule.

Accession: 008062499

Download citation: RISBibTeXText

PMID: 7766601

DOI: 10.1021/bi00021a003

Download PDF Full Text: A partially folded Intermediate during tubulin unfolding: Its detection and spectroscopic characterization



Related references

Equilibrium unfolding of partially folded staphylococcal nuclease A2- and A3-forms is accompanied by the formation of an intermediate state. Biochemistry. Biokhimiia 63(4): 470-475, 1998

Fluoroalcohols induced unfolding of Succinylated Con A: native like beta-structure in partially folded intermediate and alpha-helix in molten globule like state. Archives of Biochemistry and Biophysics 454(2): 170-180, 2006

Equilibrium unfolding of Escherichia coli ribonuclease H: characterization of a partially folded state. Protein Science 3(9): 1401-1408, 1994

Accumulation of partly folded states in the equilibrium unfolding of ervatamin A: spectroscopic description of the native, intermediate, and unfolded states. Biochimie 89(11): 1416-1424, 2007

Characterization of a partially folded intermediate of stem bromelain at low pH. European Journal of Biochemistry 269(1): 47-52, January, 2002

Characterization of a partially folded intermediate of papain induced by fluorinated alcohols at low pH. Archives of Biochemistry and Biophysics 432(1): 79-87, 2004

Characterization and analysis of binding of Thioflavin T with partially folded and native states of α-lactalbumin protein by calorimetric and spectroscopic techniques. International Journal of Biological Macromolecules 95(): 376-384, 2016

Local fluctuations and global unfolding of partially folded BPTI detected by NMR. Biophysical Chemistry. 64(1-3): 45-57, 1997

The stabilization of partially folded intermediates in the urea induced unfolding of rnase a. AAAS (American Association for the Advancement of Science) Publication (88-30): 198, 1988

The unfolding of alpha-momorcharin proceeds through the compact folded intermediate. Journal of Biochemistry 144(4): 457-466, 2008

Unfolding Energetics of G-a-Actin: A Discrete Intermediate can be Re-folded to the Native State by CCT. Journal of Molecular Biology 353(2): 5-96, 2005