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Eur J Mass Spectrom (Chichester) ; 15(2): 113-30, 2009.
Article in English | MEDLINE | ID: mdl-19423898

ABSTRACT

Detailed knowledge of the tertiary and quaternary structure of proteins and protein complexes is of immense importance in understanding their functionality. Similarly, variations in the conformational states of proteins form the underlying mechanisms behind many biomolecular processes, numerous of which are disease-related. Thus, the availability of reliable and accurate biophysical techniques that can provide detailed information concerning these issues is of paramount importance. Ion mobility spectrometry (IMS) coupled to mass spectrometry (MS) offers a unique opportunity to separate multi-component biomolecular entities and to measure the molecular mass and collision cross-section of individual components in a single, rapid (

Subject(s)
Mass Spectrometry/methods , Peptides/chemistry , Proteins/chemistry , Spectrometry, Mass, Electrospray Ionization/methods , Calibration , Mass Spectrometry/instrumentation , Protein Conformation , Protein Denaturation , Protein Folding , Reproducibility of Results , Spectrometry, Mass, Electrospray Ionization/instrumentation , Time Factors
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