Structure of the globular protein vicilin revealed by scanning tunnelling microscopy.
Scanning tunnelling microscopy (s.t.m.) has been used to study the structure of the non-crystalline globular protein vicilin. Molecules were deposited on amorphous carbon substrates and imaged both in air and in vacuo without additional sample preparation. Current-voltage plots of an individual protein molecule are also reported. The s.t.m. images are compared with conventional transmission electron micrographs and with a model of vicilin based on small-angle synchrotron X-ray scattering data.
Welland
M E
ME
Department of Engineering, Cambridge, UK.
Miles
M J
MJ
Lambert
N
N
Morris
V J
VJ
Coombs
J H
JH
Pethica
J B
JB
D004553:Electric Conductivity; D008854:Microscopy, Electron; D016252:Microscopy, Scanning Tunneling; D010940:Plant Proteins; D014674:Plant Proteins, Dietary / Q000648:ultrastructure*; D055314:Seed Storage Proteins; D014961:X-Ray Diffraction
D010940:Plant Proteins; D014674:Plant Proteins, Dietary; D055314:Seed Storage Proteins; C015575:vicilin protein, plant