Abstract
AbstractAnalysis of intact proteins is hampered by the fact that even when using high-resolution techniques, like electrospray mass spectrometry, you will only be able to tell whether the protein has the expected mass. If you find a deviation from the expected you will, in most cases, be left wondering where (and perhaps what) the difference is. These observations are compounded when using low-resolution techniques like gel filtration or sodium dodecyl sulfate (SDS) gel electrophoresis. Although 2D gel electrophoresis is able to show a single charge difference, in the absence of additional information you are still left wondering where and what the differences are.KeywordsAmino Acid AnalysisDisulfide BridgeIntact ProteinPeptide MappingDigestion TimeThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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