Scanning probe microscopy of collagen I and pN-collagen I assemblies and the relevance to scanning tunnelling microscopy contrast generation in proteins

LJ Gathercole, MJ Miles, TJ McMaster, DF Holmes

Research output: Contribution to journalArticle (Academic Journal)peer-review

24 Citations (Scopus)

Abstract

Scanning tunnelling microscopy (STM) and atomic force microscopy (AFM) have been carried out on hydrated fibrous assemblies of collagen I and pN-collagen I. STM of calf-skin collagen I that had been allowed to assemble on a graphite substrate showed the predicted 8 nm diameter microfibrils, arrays of which showed a 67 nm repeat. A detailed contrast variation along the microfilbrils was observed, corresponding to the established stain banding observed by transmission electron microscopy (TEM) and associated with hydrophilic, charged amino acid side chains along the staggered-molecule microfibril. This indicates that adsorbed water is an important mediator of STM imaging in insulators such as proteins. AFM images were obtained of D-periodic assemblies of pN-collagen deposited on carbon-coated copper TEM grids. The use of carbon-coated TEM grids as an SPM substrate allows experiments to be performed on the same samples, and correlation made between TEM and SPM images.
Translated title of the contributionScanning probe microscopy of Collagen I and pN-collagen I assemblies and the relevance to scanning tunnelling microscopy contrast generation in proteins
Original languageEnglish
Pages (from-to)2589-2594
Number of pages5
JournalJournal of the Chemical Society, Faraday Transactions
Volume89
Issue number15
DOIs
Publication statusPublished - 1993

Fingerprint Dive into the research topics of 'Scanning probe microscopy of collagen I and pN-collagen I assemblies and the relevance to scanning tunnelling microscopy contrast generation in proteins'. Together they form a unique fingerprint.

Cite this