Article
Open source platform for the execution and analysis of mechanical refolding experiments.
Department of Biochemistry G.Moruzzi, University of Bologna, Via Irnerio 48, 40126 Bologna, Italy.
Bioinformatics (impact factor:
5.47).
02/2011;
27(3):423-5.
DOI:10.1093/bioinformatics/btq663
pp.423-5
Source: PubMed
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Citations (0)
- Cited In (1)
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Article: Atomic force microscopy and spectroscopy of native membrane proteins.
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ABSTRACT: Membrane proteins comprise 30% of the proteome of higher organisms. They mediate energy conversion, signal transduction, solute transport and secretion. Their native environment is a bilayer in a physiological buffer solution, hence their structure and function are preferably assessed in this environment. The surface structure of single membrane proteins can be determined in buffer solutions by atomic force microscopy (AFM) at a lateral resolution of less than 1 nm and a vertical resolution of 0.1-0.2 nm. Moreover, single proteins can be directly addressed, stuck to the AFM stylus and subsequently unfolded, revealing the molecular interactions of the protein studied. The examples discussed here illustrate the power of AFM in the structural analysis of membrane proteins in a native environment.Nature Protocol 02/2007; 2(9):2191-7. · 8.36 Impact Factor
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Keywords
adaptable
AFM
AFM setups
AFM-independent software module
analyse mechanical refolding experiments
Apache License 2.0
atomic force microscope
biomolecular force-coupled kinetics
commercial AFM setup 'Picoforce AFM'
Digital Instruments
discrepancy
experimental investigation
explicit theoretical models
improved method
mechanical protein refolding studies
protein folding kinetics
Single-molecule force spectroscopy