SOLUTION STRUCTURE OF APOCYTOCHROME B(562)

Citation
Yq. Feng et al., SOLUTION STRUCTURE OF APOCYTOCHROME B(562), Nature structural biology, 1(1), 1994, pp. 30-35
Citations number
42
Categorie Soggetti
Biology,"Cytology & Histology
Journal title
ISSN journal
10728368
Volume
1
Issue
1
Year of publication
1994
Pages
30 - 35
Database
ISI
SICI code
1072-8368(1994)1:1<30:SSOAB>2.0.ZU;2-D
Abstract
The apoprotein is an important intermediate on the folding pathways of many haem proteins, yet a detailed structure of such an intermediate has remained elusive. Here we present the structure of apocytochrome b (562) obtained by NMR spectroscopy. The apoprotein has a topology simi lar to the holoprotein. Nevertheless, significant differences in helix -helix packing between the two are evident. Much of the haem binding p ocket in the apoprotein is preserved but exposed to solvent creating a large cavern. As apocytochrome b(562) displays many of the physical c haracteristics ascribed to the molten globule state, these results hel p ellucidate the origin of several properties of the protein molten gl obule.