Journal
ANALYTICAL CHEMISTRY
Volume 84, Issue 2, Pages 867-870Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ac202818m
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Funding
- Grant Agency of the Czech Republic [P207/10/1040, 303/09/0477, 305/09/H008]
- Ministry of Education, Youth and Sports of the Czech Republic [LC545]
- Academy of Sciences of the Czech Republic [AV0Z50200510, AV0Z50520701]
- Grant Agency of Charles University [403211/2011]
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A combination of chemical cross-linking and hydrogen-deuterium exchange coupled to high resolution mass spectrometry was used to describe structural differences of NKR-P1A receptor. The loop region extended from the compact core in the crystal structure was found to be closely attached to the protein core in solution. Our approach has potential to refine protein structures in solution within a few days and has very low sample consumption.
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