Issue 7, 2004
From the journal:

Physical Chemistry Chemical Physics

Thermophoresis as a probe of particle–solvent interactions: The case of protein solutions†

Roberto Piazza,*a   Sara Iacopiniab  and  Benedetta Triulziab  

* Corresponding authors

a Dipartimento di Ingegneria Nucleare, Politecnico di Milano, via Ponzio 34/3, Milano, Italy
E-mail: roberto.piazza@polimi.it

b Dipartimento di Fisica, Università di Milano, via Celoria 16, 20133 Milano, Italy

Abstract

Thermophoresis, or thermal diffusion, consists in particle drift induced by thermal gradients. We discuss the physical mechanisms underlying thermophoresis in colloidal suspensions and macromolecular solutions, and present a general model suggesting thermophoretic measurements as a sensitive probe of particle–solvent interfacial properties. After reviewing recent results obtained by our group on thermal diffusion in charged colloidal systems, we discuss thermophoresis in protein solutions as a specific ‘case study’.

About
Cited by
Related
Download options Please wait...

Article information

DOI
https://doi.org/10.1039/B312856C
Article type
Paper
Submitted
14 Oct 2003
Accepted
23 Dec 2003
First published
28 Jan 2004

Phys. Chem. Chem. Phys., 2004,6, 1616-1622

Permissions

Request permissions

Thermophoresis as a probe of particle–solvent interactions: The case of protein solutions

R. Piazza, S. Iacopini and B. Triulzi, Phys. Chem. Chem. Phys., 2004, 6, 1616 DOI: 10.1039/B312856C

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements