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Randolph V. Norheim

Researcher at Pacific Northwest National Laboratory

Publications -  31
Citations -  1296

Randolph V. Norheim is an academic researcher from Pacific Northwest National Laboratory. The author has contributed to research in topics: Ion & Ion-mobility spectrometry. The author has an hindex of 18, co-authored 28 publications receiving 973 citations. Previous affiliations of Randolph V. Norheim include Environmental Molecular Sciences Laboratory.

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Ultra-High Resolution Ion Mobility Separations Utilizing Traveling Waves in a 13 m Serpentine Path Length Structures for Lossless Ion Manipulations Module.

TL;DR: The development and initial evaluation of a 13 m path length Structures for Lossless Manipulations (SLIM) module for achieving high resolution separations using traveling waves (TW) with ion mobility (IM) spectrometry and it provides a foundation for the development of much higher resolution SLIM devices based upon both considerably longer path lengths and multipass designs.
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Experimental Evaluation and Optimization of Structures for Lossless Ion Manipulations for Ion Mobility Spectrometry with Time-of-Flight Mass Spectrometry

TL;DR: Both geometries provide IMS resolving powers at the theoretical limit (R ∼ 58) showing that degraded resolution from a “racetrack” effect from turning around a corner can be successfully avoided, and the capability also was maintained for essentially lossless ion transmission.
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Development of a new ion mobility time-of-flight mass spectrometer

TL;DR: In this article, a new ion mobility spectrometer (IMS) platform was developed to improve upon the sensitivity and reproducibility of previous platforms, and further enhance IMS-MS utility for broad 'panomics' measurements.
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Ion Mobility Separations of Isomers based upon Long Path Length Structures for Lossless Ion Manipulations Combined with Mass Spectrometry.

TL;DR: A new approach using Structures for Lossless Ion Manipulations (SLIM) to enable long serpentine path ion mobility spectrometry (IMS) separations followed by MS analyses, which provides previously unachieved resolution for biomolecular species, in conjunction with more effective ion utilization.