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Comparative investigation of PdR by usual and ultrafine atomic force microscopy

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Analytical Methods Vol - 2 Issue - 5

Analytical Methods Vol - 2 Issue - 4

Analytical Methods Vol - 2 Issue - 3

Analytical Methods Vol - 2 Issue - 2

Analytical Methods Vol -1

Comparative investigation of PdR by usual and ultrafine atomic force microscopy

Content Provider	Royal Society of Chemistry (RSC)
Author	Bykov, Victor A. Besedin, Stanislav P. Hoa, Gaston Hui Bon Frantsuzov, Pavel A. Ivanov, Yuri D. Archakov, Alexander I.
Copyright Year	2010
Abstract	Atomic force microscopy is one of the most perspective methods for determination of the structure of proteins and their complexes. The vertical resolution of this method is about 0.1 nm, which is close to X-ray resolution. At the same time, the lateral resolution, determining by broadening effect of a standard AFM probe, is not very high—about 20–50 nm, depending on probe geometry. Naturally, the probe tip broadening effect leads to substantial enhancement of measured protein volume. In this study, a comparative analysis of sizes of the protein putidaredoxin reductase (PdR) obtained by the use of two AFM probe types, standard and supersharp, was undertaken. Usage of standard probes enabled to correctly measure the height of PdR while the volume of this protein was measured with considerably (more than one order) enhancement. It was shown that application of supersharp AFM probes results in the lowering of measured protein height; at the same time, the measured protein volume is more exact and appears to be close to RSA data. Therefore, to obtain exact data on protein volume and height, these two parameters should be measured by use of both supersharp probes and standard geometry probes.
Starting Page	688
Ending Page	693
Page Count	6
File Format	HTM / HTML PDF
ISSN	17599660
Volume Number	2
Issue Number	6
Journal	Analytical Methods
DOI	10.1039/b9ay00274j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	X-ray crystallography Atomic-force microscopy RSA Security Protein Molecular geometry
Content Type	Text
Resource Type	Article
Subject	Analytical Chemistry Engineering Chemical Engineering

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3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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