Imaging the molecular dimensions and oligomerization of proteins at liquid/solid interfaces

Journal of Physical Chemistry B

Volumn 102, Issue 9, 1998, Pages 1649-1657

  Waner, Mark J ^a   Gilchrist, Martha ^a   Schindler, Melvin ^b   Dantus, Marcos ^a  

^a MICHIGAN STATE UNIVERSITY   (United States)

^b Michigan State University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADSORPTION; ATOMIC FORCE MICROSCOPY; MOLECULAR ORIENTATION; MOLECULAR STRUCTURE; OLIGOMERS; PHASE INTERFACES; POLYMERIZATION;

OLIGOMERIZATION;

PROTEINS;

EID: 0031997948     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp9732219     Document Type: Article

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46. 39 For particles with a diameter of 40 Å, the maximum height deviation can be as much as 0.7 Å. We have modeled this effect by calculating the average error expected given 500 randomly placed 40 Å diameter spheres. (Spherical geometry maximizes this resolution effect.) The average error obtained from our simulation was 0.2 Å, which amounts to 0.5% error in the height measurement of the particles. This error is smaller than the natural roughness of atomicaliy flat mica; therefore, no attempt was made to minimize it or correct for it.
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56. The origin of this variability is currently under investigation. Some of the variation may be attributed to the amount of background noise, perhaps due to differences in the mica substrate or changes in instrument performance. Capillary forces may also play a role in this variability. Further experiments, carried out under liquid conditions, will help us make this assessment.