Structural Changes in Tubulin Sheets Caused by Immobilization on Solid Supports.

ABSTRACT: In the presence of zinc, the protein tubulin assembles into two-dimensional sheets that are a useful model system for the study of both tubulin and microtubule structure. Tubulin sheets present an ideal protein structure for study with atomic force microscopy because they contain a two-dimensional crystalline protein lattice and retain many of the structural features of tubulin and microtubules. However, high-resolution imaging requires nonperturbative immobilization onto an appropriate imaging substrate. In this report, several substrates commonly used for scanning probe microscopy are evaluated for their ability to effectively immobilize tubulin sheets: mica, gold, highly ordered pyrolytic graphite, and carbon-coated electron microscopy grids. We hypothesize that the different intermolec

SUBMITTER: Donhauser ZJ 

PROVIDER: S-EPMC6312633 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature