View publication

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

(click to unfold)
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 
Models, Molecular Deuterium Exchange Measurement Magnetic Resonance Spectroscopy Amides Caenorhabditis elegans Molecular Sequence Data Protein Conformation Time Factors Caenorhabditis elegans Proteins Animals Mass Spectrometry Amino Acid Sequence Proteins Bacteria Escherichia coli Proteins Nerve Tissue Proteins 
19306341  
10.1002/prot.22394  
24 (Last update: 05/27/2017 11:17:39am)  
Construct optimization for protein NMR structure analysis using amide hydrogen/deuterium exchange mass spectrometry
 
method