Imaging proteins with atomic force microscopy: an overview

Atomic force microscopy (AFM) has become a common tool for biophysical studies of proteins; mainly due its property to perform characterizations near physiological conditions. The tertiary and quaternary structures, forces driving folding-unfolding processes, and secondary structure elements can be...

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Bibliographic Details
Published inCurrent protein & peptide science Vol. 6; no. 4; p. 387
Main Author Silva, Luciano Paulino
Format Journal Article
LanguageEnglish
Published United Arab Emirates 01.08.2005
Subjects
Crystallography, X-Ray
DNA - chemistry
DNA - metabolism
DNA - ultrastructure
Ligands
Microscopy, Atomic Force - methods
Protein Folding
Proteins - chemistry
Proteins - metabolism
Proteins - ultrastructure
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Summary:Atomic force microscopy (AFM) has become a common tool for biophysical studies of proteins; mainly due its property to perform characterizations near physiological conditions. The tertiary and quaternary structures, forces driving folding-unfolding processes, and secondary structure elements can be studied in their native environments allowing high resolution level associated with small distortions. This review outlines the operational principles and applications of AFM for protein biophysics.
ISSN:1389-2037
DOI:10.2174/1389203054546389