Motions of Single Molecules and Proteins in Trehalose Glass

7 February 2003

journal article
Published by American Chemical Society (ACS) in Journal of the American Chemical Society

Vol. 125 (9) , 2730-2735
https://doi.org/10.1021/ja021197t

Abstract

The fluorescence intensity−time records of individual metal-free porphyrin cytochrome-c and Zn porphyrin cytochrome-c molecules whose translational motions are restricted by encapsulation in trehalose are examined by single-molecule spectroscopy by means of a two-channel confocal microscope that records transient fluorescence signals in two orthogonal polarization directions. Large angular motions often occur on time scales ranging to many seconds. Measurements of the photobleaching time distributions indicate that the trehalose glass restricts the accessibilty of the fluorescent molecules to oxygen.

Keywords

This publication has 20 references indexed in Scilit:

Single-Molecule Studies of Heterogeneous Dynamics in Polymer Melts Near the Glass Transition
Science, 2001
Effect of Trehalose on Alkaline Transition of Cytochrome-c
The Journal of Physical Chemistry B, 2000
Illuminating Single Molecules in Condensed Matter
Science, 1999
Water hydrogen-bond dynamics close to hydrophobic and hydrophilic groups
Faraday Discussions, 1996
Geminate Rebinding and Conformational Dynamics of Myoglobin Embedded in a Glass at Room Temperature
The Journal of Physical Chemistry, 1996
Overview lecture. Hydration processes in biological and macromolecular systems
Faraday Discussions, 1996
Photophysical Properties and Photochemical Stability of Rhodamine B Encapsulated in SiO2 and Si-Ti Binary Oxide Matrixes by the Sol-Gel Method
Langmuir, 1994
Room Temperature Trapping of Rhodopsin Photointermediates
Biochemistry, 1994
An infrared spectroscopic study of the interactions of carbohydrates with dried proteins
Biochemistry, 1989
Metallocytochromes c : Characterization of Electronic Absorption and Emission Spectra of Sn4+ and Zn2+ Cytochromes c
European Journal of Biochemistry, 1976