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

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

doi:10.1021/bi500420y

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

Ying Zhang
, Erica L.W. Majumder
, Hai Yue
, Robert E. Blankenship
, Michael L. Gross

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

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.

Original language	English
Pages (from-to)	5619-5630
Number of pages	12
Journal	Biochemistry
Volume	53
Issue number	35
DOIs	https://doi.org/10.1021/bi500420y
State	Published - Sep 9 2014

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title = "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.",

author = "Ying Zhang and Majumder, \{Erica L.W.\} and Hai Yue and Blankenship, \{Robert E.\} and Gross, \{Michael L.\}",

note = "Publisher Copyright: {\textcopyright} 2014 American Chemical Society.",

year = "2014",

month = sep,

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doi = "10.1021/bi500420y",

language = "English",

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pages = "5619--5630",

journal = "Biochemistry",

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T1 - Structural analysis of diheme cytochrome c by hydrogen-deuterium exchange mass spectrometry and homology modeling

AU - Zhang, Ying

AU - Majumder, Erica L.W.

AU - Yue, Hai

AU - Blankenship, Robert E.

AU - Gross, Michael L.

PY - 2014/9/9

Y1 - 2014/9/9

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/84907519228

U2 - 10.1021/bi500420y

DO - 10.1021/bi500420y

M3 - Article

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AN - SCOPUS:84907519228

SN - 0006-2960

VL - 53

SP - 5619

EP - 5630

JO - Biochemistry

JF - Biochemistry

IS - 35

ER -

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

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