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Structural analysis of diheme cytochrome c by hydrogen-deuterium exchange mass spectrometry and homology modeling.


ABSTRACT: A lack of X-ray or nuclear magnetic resonance structures of proteins inhibits their further study and characterization, motivating the development of new ways of analyzing structural information without crystal structures. The combination of hydrogen-deuterium exchange mass spectrometry (HDX-MS) data in conjunction with homology modeling can provide improved structure and mechanistic predictions. Here a unique diheme cytochrome c (DHCC) protein from Heliobacterium modesticaldum is studied with both HDX and homology modeling to bring some definition of the structure of the protein and its role. Specifically, HDX data were used to guide the homology modeling to yield a more functionally relevant structural model of DHCC.

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC4159202 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature

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Structural analysis of diheme cytochrome c by hydrogen-deuterium exchange mass spectrometry and homology modeling.

Zhang Ying Y   Majumder Erica L-W EL   Yue Hai H   Blankenship Robert E RE   Gross Michael L ML  

Biochemistry 20140827 35


A lack of X-ray or nuclear magnetic resonance structures of proteins inhibits their further study and characterization, motivating the development of new ways of analyzing structural information without crystal structures. The combination of hydrogen-deuterium exchange mass spectrometry (HDX-MS) data in conjunction with homology modeling can provide improved structure and mechanistic predictions. Here a unique diheme cytochrome c (DHCC) protein from Heliobacterium modesticaldum is studied with b  ...[more]

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