Thinner, smaller, faster: IR techniques to probe the functionality of biological and biomimetic systems

Angew Chem Int Ed Engl. 2010 Jul 26;49(32):5416-24. doi: 10.1002/anie.200907114.

Abstract

New techniques in vibrational spectroscopy are promising for the study of biological samples as they provide exquisite spatial and/or temporal resolution with the benefit of minimal perturbation of the system during observation. In this Minireview we showcase the power of modern infrared techniques when applied to biological and biomimetic systems. Examples will be presented on how conformational changes in peptides can be traced with femtosecond resolution and nanometer sensitivity by 2D IR spectroscopy, and how surface-enhanced infrared difference absorption spectroscopy can be used to monitor the effect of the membrane potential on a single proton-transfer step in an integral membrane protein. Vibrational spectra of monolayers of molecules at basically any interface can be recorded with sum-frequency generation, which is strictly surface-sensitive. Chemical images are recorded by applying scanning near-field infrared microscopy at lateral resolutions better than 50 nm.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Biomimetic Materials / chemistry
  • Humans
  • Proteins / chemistry
  • Spectrophotometry, Infrared / economics
  • Spectrophotometry, Infrared / instrumentation
  • Spectrophotometry, Infrared / methods*

Substances

  • Proteins