Protein elasticity probed with two synchrotron-based techniques.
J Chem Phys
; 132(8): 085103, 2010 Feb 28.
Article
em En
| MEDLINE
| ID: mdl-20192318
ABSTRACT
Compressibility characterizes three interconnecting properties of a protein dynamics, structure, and function. The compressibility values for the electron-carrying protein cytochrome c and for other proteins, as well, available in the literature vary considerably. Here, we apply two synchrotron-based techniques--nuclear resonance vibrational spectroscopy and inelastic x-ray scattering--to measure the adiabatic compressibility of this protein. This is the first report of the compressibility of any material measured with this method. Unlike the methods previously used, this novel approach probes the protein globally, at ambient pressure, does not require the separation of protein and solvent contributions to the total compressibility, and uses samples that contain the heme iron, as in the native state. We show, by comparing our results with molecular dynamics predictions, that the compressibility is almost independent of temperature. We discuss potential applications of this method to other materials beyond proteins.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Grupo dos Citocromos c
/
Elasticidade
Limite:
Animals
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article