Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.
 

Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.

Related Articles Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.

Biochim Biophys Acta. 2000 Aug 30;1460(1):39-48

Authors: Saitô H, Tuzi S, Yamaguchi S, Tanio M, Naito A

It is demonstrated here how the secondary structure and dynamics of transmembrane helices, as well as surface residues, such as interhelical loops and N- or C-terminus of bacteriorhodopsin (bR) in purple membrane, can be determined at ambient temperature based on very simple (13)C-NMR measurements, together with a brief experimental background. In contrast to the static picture of bR, currently available from X-ray diffraction or cryo-electron microscopy, the structure consists of dynamically heterogeneous domains which undergo various types of local fluctuations with a frequency range of 10(2)--10 (8) Hz. The significance of this picture is discussed in relation to the biological function of this protein.

PMID: 10984589 [PubMed - indexed for MEDLINE]



Source: PubMed