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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lohr, D. Bash, R. Wang, H. Yodh, J. Lindsay, S. |
| Description | Country affiliation: United States Author Affiliation: Lohr D ( Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604, USA. dlohr@asu.edu) |
| Abstract | Atomic force microscopy (AFM) is a technique that can directly image single molecules in solution and it therefore provides a powerful tool for obtaining unique insights into the basic properties of biological materials and the functional processes in which they are involved. We have used AFM to analyze basic features of nucleosomes in arrays, such as DNA-histone binding strength, cooperativity in template occupation, nucleosome stabilities, nucleosome locations and the effects of acetylation, to compare these features in different types of arrays and to track the response of array nucleosomes to the action of the human Swi-Snf ATP-dependent nucleosome remodeling complex. These experiments required several specific adaptations of basic AFM methods, such as repetitive imaging of the same fields of molecules in liquid, the ability to change the environmental conditions of the sample being imaged and detection of specific types of molecules within compositionally complex samples. Here, we describe the techniques that allowed such analyses to be carried out. |
| File Format | HTM / HTML |
| ISSN | 10462023 |
| e-ISSN | 10959130 |
| Journal | Methods |
| Issue Number | 3 |
| Volume Number | 41 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2007-03-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Discipline Life sciences, Biochemistry Chromatin Assembly And Disassembly Physiology Microscopy, Atomic Force Nucleosomes Chemistry Acetylation Dna-binding Proteins Genetics Metabolism Histones Instrumentation Transcription Factors |
| Content Type | Text |
| Resource Type | Article |
| Subject | Molecular Biology |
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