Several prior-art techniques such as ion mobility spectrometry and gas-phase HDX measurements have been used for assessing the conformational properties of gaseous protein ions. Most of these approaches comprise the use of ion traps or ICR cells where a gas is introduced and the ions are incubated with the gas. However, such approaches are associated with potential limitations such as extended gas-phase labeling time, complex exchange kinetics, and comparatively low gas pressure. This novel approach enables a rapid gas-phase isotopic labeling of protein ions for enhanced detection of protein conformations.
Value Proposition
The approach:
•Involves use of a curtain labeling technique wherein the protein ions are allowed to pass through a cloud of deuterated gas for labeling
•Allows for an effective control over gas-phase labeling time along with obtaining higher operational gas pressure as compared to conventional techniques
•Offers unique advantages and flexibility for analytical measurements over prior-art approaches
•Would be commercially useful for determination of protein stoichiometry along with architecturing of large functional protein assemblies
Intellectual Property status
Pending Utility Application 13/264,574
Pending Canada National Application 2,758,917
Pending European National Application 10765098.8
License status
Available for license
Direct Link:http://neu.technologypublisher.com/technology/20052
Northeastern University is a private national research university located in Boston, Massachusetts. Northeastern is a leader in worldwide experiential learning, urban engagement, and interdisciplinary research that meets global and societal needs. The University offers a comprehensive range of undergraduate and graduate programs leading to degrees through the doctorate in nine colleges and schools. Areas of technology research and development range across the Life Sciences and Material Sciences.
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