Solution structure of apocytochrome B562

Yiqing Feng, Stephen G. Sligar, A. Joshua Wand

Research output: Contribution to journalArticlepeer-review

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 Jb562 obtained by NMR spectroscopy. The apoprotein has a topology similar to the holoprotein. Nevertheless, significant differences in helix-helix packing between the two are evident. Much of the haem binding pocket in the apoprotein is preserved but exposed to solvent creating a large cavern. As apocytochrome b562 displays many of the physical characteristics ascribed to the molten globule state, these results help ellucidate the origin of several properties of the protein molten globule.

Original languageEnglish (US)
Pages (from-to)30-35
Number of pages6
JournalNature Structural Biology
Volume1
Issue number1
DOIs
StatePublished - Jan 1994

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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