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      Atomic Force Microscopy for Protein Detection and Their Physicoсhemical Characterization

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          Abstract

          This review is focused on the atomic force microscopy (AFM) capabilities to study the properties of protein biomolecules and to detect the proteins in solution. The possibilities of application of a wide range of measuring techniques and modes for visualization of proteins, determination of their stoichiometric characteristics and physicochemical properties, are analyzed. Particular attention is paid to the use of AFM as a molecular detector for detection of proteins in solutions at low concentrations, and also for determination of functional properties of single biomolecules, including the activity of individual molecules of enzymes. Prospects for the development of AFM in combination with other methods for studying biomacromolecules are discussed.

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          Most cited references138

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          Atomic Force Microscope

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            Single Molecule Force Spectroscopy on Polysaccharides by Atomic Force Microscopy

            Recent developments in piconewton instrumentation allow the manipulation of single molecules and measurements of intermolecular as well as intramolecular forces. Dextran filaments linked to a gold surface were probed with the atomic force microscope tip by vertical stretching. At low forces the deformation of dextran was found to be dominated by entropic forces and can be described by the Langevin function with a 6 angstrom Kuhn length. At elevated forces the strand elongation was governed by a twist of bond angles. At higher forces the dextran filaments underwent a distinct conformational change. The polymer stiffened and the segment elasticity was dominated by the bending of bond angles. The conformational change was found to be reversible and was corroborated by molecular dynamics calculations.
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              Single-molecule studies of DNA mechanics.

              During the past decade, physical techniques such as optical tweezers and atomic force microscopy were used to study the mechanical properties of DNA at the single-molecule level. Knowledge of DNA's stretching and twisting properties now permits these single-molecule techniques to be used in the study of biological processes such as DNA replication and transcription.
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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                MDPI
                1422-0067
                10 April 2018
                April 2018
                : 19
                : 4
                : 1142
                Affiliations
                Institute of Biomedical Chemistry, 10, Pogodinskaya St., 119121 Moscow, Russia; t.pleshakova@ 123456gmail.com (T.O.P.); natalie_buharina@ 123456list.ru (N.S.B.); alexander.archakov@ 123456ibmc.msk.ru (A.I.A.)
                Author notes
                Author information
                https://orcid.org/0000-0003-3217-9095
                Article
                ijms-19-01142
                10.3390/ijms19041142
                5979402
                29642632
                482d3739-380d-4ef3-a88e-d6d07150ef65
                © 2018 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 26 February 2018
                : 05 April 2018
                Categories
                Review

                Molecular biology
                atomic force microscopy,protein fishing,protein characterization
                Molecular biology
                atomic force microscopy, protein fishing, protein characterization

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