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Int. J. Mol. Sci. 2001, 2(2), 109-120; doi:10.3390/i2020109

Glycerol-Induced Aggregation of the Oligomeric L-Asparaginase II from E. coli Monitored with ATR-FTIR

Institüt für Physiologische Chemie der Philipps Universität, Karl-von-Frisch Str.1, D-35033 Marburg, Germany
Received: 9 April 2001 / Accepted: 15 June 2001 / Published: 28 June 2001
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Abstract

In this paper attenuated total reflectance Fourier transform infrared spectroscopy has been employed for the study of the structural composition of aggregates of the oligomeric L-asparaginase II from E.coli formed in the presence of glycerol after the induction of refolding of the protein. Apart from the perfect coincidence of the secondary structure composition of EcA2 as determined by FTIR and crystallography [1], it has also been shown that secondary structure of protein in asparaginase deposits is similar to that of the native conformation: 20.7% extended, 22.3% disordered, 31.4% helix and 25.6% turn/bend/β sheet. Certain structural similarities in the range of experimental error was observed for all three protein deposits presented in this paper, indicating a common structural basis for the composition of this types of aggregates. It is concluded that in the constitution of such precipitates, a partially folded (molten globule like) state(s) is involved, and its stabilisation is a key factor leading to the aggregation. The results presented in this paper might serve to be a good explanation and an excellent basis for the fundamental theory of protein (oligomers) precipitation by osmotic substances. View Full-Text
Keywords: attenuated total reflectance Fourier transform infrared spectroscopy; the oligomeric L-asparaginase II; secondary structure attenuated total reflectance Fourier transform infrared spectroscopy; the oligomeric L-asparaginase II; secondary structure
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Adeishvili, K. Glycerol-Induced Aggregation of the Oligomeric L-Asparaginase II from E. coli Monitored with ATR-FTIR. Int. J. Mol. Sci. 2001, 2, 109-120.

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