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Transient Interaction with Nanoparticles "Freezes" a Protein in an Ensemble of Metastable Near-Native Conformations:  
Umeå University, Faculty of Science and Technology, Chemistry.
2005 (English)In: Biochemistry including biophysical chemistry& molecular biology, Vol. 44, no 30, 10093-9 p.Article in journal (Refereed) Published
Abstract [en]


It is well-known that adsorption of proteins on interfaces often induces substantial alterations of the protein structure. However, very little is known about whether these conformational changes have any consequence for the protein conformation after desorption from the interface. To investigate this matter, we have selected a protein-particle system in which the enzyme human carbonic anhydrase I (HCAI) alternates between the adsorbed and free state upon interaction with the silica nanoparticles. High-resolution NMR analysis of the protein with the particles present in the sample shows a spectrum that indicates a molten globular-like structure. Removal of particles results in refolding of virtually all HCAI molecules to a fully active form. However, the two-dimensional NMR analysis shows that refolding does not result in a single well-defined protein structure but rather provides an ensemble of protein molecules with near-native conformations. A detailed comparative chemical shift analysis of 108 amide signals in 1H-15N HSQC spectra of native and desorbed HCAI reveals that the most profound effects are located at β-strands in the center of the molecule. The observation of very slow H-D exchange in the central β-strands of HCAI [Kjellsson, A., Sethson, I., and Jonsson, B. H. (2003) Biochemistry 42, 363-374] in conjunction with our results indicates that the kinetic barriers for conformational rearrangements in the central core of the protein are low in the presence of nanoparticles but are very high under native conditions.

Place, publisher, year, edition, pages
ACS Publications , 2005. Vol. 44, no 30, 10093-9 p.
URN: urn:nbn:se:umu:diva-22981DOI: 10.1021/bi0500067OAI: diva2:218901
Available from: 2009-05-25 Created: 2009-05-25 Last updated: 2009-05-25Bibliographically approved

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ReferencesLink to record
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