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Construct optimization for protein NMR structure analysis using amide hydrogen/deuterium exchange mass spectrometry.

Sharma S, Zheng H, Huang YJ, Ertekin A, Hamuro Y, Rossi P, Tejero R, Acton TB, Xiao R, Jiang M, Zhao L, Ma LC, Swapna GV, Aramini JM, Montelione GT,
Proteins (2009) 76:882-894 PublishedPSI:Phase 2  
Northeast Structural Genomics Consortium

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Disordered or unstructured regions of proteins, while often very important biologically, can pose significant challenges for resonance assignment and three-dimensional structure determination of the ordered regions of proteins by NMR methods. ...
chemistry methods economics 
Amino Acid Sequence Animals Models, Molecular Molecular Sequence Data Nerve Tissue Proteins Proteins Escherichia coli Proteins Mass Spectrometry Protein Conformation Bacteria Time Factors Amides Magnetic Resonance Spectroscopy Caenorhabditis elegans Caenorhabditis elegans Proteins Deuterium Exchange Measurement 
19306341  
10.1002/prot.22394  
25 (Last update: 11/17/2018 12:13:42pm)  
Construct optimization for protein NMR structure analysis using amide hydrogen/deuterium exchange mass spectrometry
 
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