Publication Date:
1995-04-07
Description:
Topographs of two-dimensional porin OmpF crystals reconstituted in the presence of lipids were recorded in solution by atomic force microscopy (AFM) to a lateral resolution of 10 angstroms and a vertical resolution of 1 angstrom. Protein-protein interactions were demonstrated on the basis of the AFM results and earlier crystallographic findings. To assess protein-lipid interactions, the bilayer was modeled with kinked lipids by fitting the head groups to contours determined with AFM. Finally, two conformations of the extracellular porin surface were detected at forces of 0.1 nanonewton, demonstrating the potential of AFM to monitor conformational changes with high resolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schabert, F A -- Henn, C -- Engel, A -- New York, N.Y. -- Science. 1995 Apr 7;268(5207):92-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Maurice E. Muller Institute for Microscopic Structural Biology, Universitat Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701347" target="_blank"〉PubMed〈/a〉
Keywords:
Crystallography, X-Ray
;
Escherichia coli/*chemistry
;
Lipid Bilayers/chemistry
;
Microscopy, Atomic Force
;
Models, Molecular
;
Molecular Conformation
;
Porins/chemistry/*ultrastructure
;
Protein Conformation
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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