Journal
MOLECULAR BIOSYSTEMS
Volume 6, Issue 9, Pages 1532-1539Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c000896f
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Funding
- NIGMS NIH HHS [R01 GM067193, R01 GM067193-07, GM 067193] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM067193] Funding Source: NIH RePORTER
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Top Down mass spectrometry (MS) has emerged as an alternative to common Bottom Up strategies for protein analysis. In the Top Down approach, intact proteins are fragmented directly in the mass spectrometer to achieve both protein identification and characterization, even capturing information on combinatorial post-translational modifications. Just in the past two years, Top Down MS has seen incremental advances in instrumentation and dedicated software, and has also experienced a major boost from refined separations of whole proteins in complex mixtures that have both high recovery and reproducibility. Combined with steadily advancing commercial MS instrumentation and data processing, a high-throughput workflow covering intact proteins and polypeptides up to 70 kDa is directly visible in the near future.
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