Structural Analysis of Diheme Cytochrome c by Hydrogen–Deuterium Exchange Mass Spectrometry and Homology Modeling | Zendy

Ying Zhang | Zendy; Erica L.W. Majumder | Zendy; Hai Yue | Zendy; Robert E. Blankenship | Zendy; Michael L. Gross | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Structural Analysis of Diheme Cytochrome c by Hydrogen–Deuterium Exchange Mass Spectrometry and Homology Modeling

Author(s) -

Ying Zhang,

Erica L.W. Majumder,

Hai Yue,

Robert E. Blankenship,

Michael L. Gross

Publication year - 2014

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.43

H-Index - 253

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/bi500420y

Subject(s) - homology modeling , hydrogen–deuterium exchange , mass spectrometry , chemistry , homology (biology) , cytochrome c , deuterium , protein structure , computational biology , crystallography , biochemistry , biology , amino acid , physics , enzyme , chromatography , mitochondrion , atomic physics

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research