Role of macromolecular assemblies in cellular assembly

Research output: Chapter in Book/Report/Conference proceedingConference contribution

1 Scopus citations

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 languageEnglish (US)
Title of host publicationAmerican Chemical Society, Polymer Preprints, Division of Polymer Chemistry
EditorsBill M. Culbertson
PublisherPubl by ACS
Pages229
Number of pages1
Volume32
Edition1
StatePublished - Apr 1991
EventPapers presented at the Atlanta Meeting 1991 of the ACS, Division of Polymer Chemistry - Atlanta, GA, USA
Duration: Apr 14 1991Apr 19 1991

Other

OtherPapers presented at the Atlanta Meeting 1991 of the ACS, Division of Polymer Chemistry
CityAtlanta, GA, USA
Period4/14/914/19/91

ASJC Scopus subject areas

  • Polymers and Plastics

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  • Cite this

    Pizziconi, V., & Page, D. (1991). Role of macromolecular assemblies in cellular assembly. In B. M. Culbertson (Ed.), American Chemical Society, Polymer Preprints, Division of Polymer Chemistry (1 ed., Vol. 32, pp. 229). Publ by ACS.