Abstract
One approach taken in this study to further elucidate adhesive macromolecular assemblies and their binding domains is the direct imaging of their structures using scanning tunneling microscopy (STM). The uniqueness of STM for the imaging of biological structures is its ability to attain molecular (and potentially atomic) resolution in an aqueous environment. A preliminary STM study of laminin, a large glycoprotein (MW = 900,000) found in the basement membrane, was conducted. A structural representation of laminin based upon EM studies reveals a crucifix-like shape having three short arms and one long arm. Preliminary findings depict a remarkably similar cruciform structure and approximate molecular dimensions of laminin. In addition, contrast (height) data appear to be coincident with the reported cell binding domains (lightest regions).
| Original language | English (US) |
|---|---|
| Title of host publication | American Chemical Society, Polymer Preprints, Division of Polymer Chemistry |
| Editors | Bill M. Culbertson |
| Publisher | Publ by ACS |
| Pages | 229 |
| Number of pages | 1 |
| Volume | 32 |
| Edition | 1 |
| State | Published - Apr 1991 |
| Event | Papers presented at the Atlanta Meeting 1991 of the ACS, Division of Polymer Chemistry - Atlanta, GA, USA Duration: Apr 14 1991 → Apr 19 1991 |
Other
| Other | Papers presented at the Atlanta Meeting 1991 of the ACS, Division of Polymer Chemistry |
|---|---|
| City | Atlanta, GA, USA |
| Period | 4/14/91 → 4/19/91 |
ASJC Scopus subject areas
- Polymers and Plastics