Long-range electrostatic trapping of single-protein molecules at a liquid-solid interface

The motion of single, dye-labeled protein molecules was monitored at various pH and ionic strengths within the 180-nanometer-thick evanescent-field layer at a fused-silica surface. Below the isoelectric point, molecules partitioning into the excitation region increased in number but maintained a random spatial distribution, implying that surface charge can influence the charged protein at distances beyond that of the electrical double-layer thickness. The residence times of the molecules in the interfacial layer also increased below the isoelectric point. However, immobilization on the solid surface for extended periods was not observed. Histograms of residence times exhibit nearly identical asymmetry as the corresponding elution peaks in capillary electrophoresis. These results are a direct verification of the statistical theory of chromatography at the single-molecule level, with the caveat that long-range trapping rather than adsorption is the dominant mechanism.

Medienart:

Artikel

Erscheinungsjahr:

1998

Erschienen:

1998

Enthalten in:

Zur Gesamtaufnahme - volume:281

Enthalten in:

Science (New York, N.Y.) - 281(1998), 5383 vom: 11. Sept., Seite 1650-3

Sprache:

Englisch

Beteiligte Personen:

Xu, X H [VerfasserIn]
Yeung, E S [VerfasserIn]

Themen:

11028-71-0
5-carboxytetramethylrhodamine succinimidyl ester
Concanavalin A
Journal Article
Proteins
Research Support, U.S. Gov't, Non-P.H.S.
Rhodamines

Anmerkungen:

Date Completed 07.10.1998

Date Revised 19.06.2019

published: Print

Citation Status MEDLINE

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM096723017