| Literature DB >> 7729557 |
A Ahmed1, H A Tajmir-Riahi, R Carpentier.
Abstract
In chloroplast photosystem II, the extrinsic polypeptide of 33 kDa is involved in the stabilization the Mn cluster in charge of water splitting and in the fulfilment of the Ca(2+)-cofactor requirement for oxygen evolution. The conformational analysis of the purified 33 kDa extrinsic polypeptide was carried out using FTIR spectroscopy with its self-deconvolution and second derivative resolution enhancement as well as curve-fitting procedures. The FTIR spectroscopic results showed that the isolated polypeptide is characterized by a major proportion beta-sheet conformation (36%) with 27% alpha-helix, 24% turn, and 13% beta-antiparallel structures.Entities:
Mesh:
Substances:
Year: 1995 PMID: 7729557 DOI: 10.1016/0014-5793(95)00282-e
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124