Protein structure determination using a combination of cross-linking, mass spectrometry, and molecular modeling.
Cross-linking in combination with mass spectrometry can be used as a tool for structural modeling of protein complexes and multidomain proteins. Although cross-links represent only weak structural constraints, the combination of a limited set of experimental cross-links with molecular docking/modeling is often sufficient to determine the structure of a protein complex or multidomain protein at low resolution.
School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Australia.
Dmitri
D
Mouradov
Gordon
G
King
Ian L
IL
Ross
Jade K
JK
Forwood
David A
DA
Hume
Andrea
A
Sinz
Jennifer L
JL
Martin
Bostjan
B
Kobe
Thomas
T
Huber
D000818:Animals; D043422:Carboxypeptidases A / Q000737:chemistry* / Q000378:metabolism; D003432:Cross-Linking Reagents / Q000737:chemistry*; D051379:Mice; D008958:Models, Molecular; D011487:Protein Conformation; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D013388:Succinimides / Q000737:chemistry*; D013869:Thiolester Hydrolases / Q000737:chemistry* / Q000378:metabolism
D003432:Cross-Linking Reagents; D013388:Succinimides; C035759:3,3'-dithiobis(sulfosuccinimidyl propionate); D013869:Thiolester Hydrolases; C447830:Acot1 protein, mouse; D043422:Carboxypeptidases A