May 15, 1997

Characterization of the structural difference between active and inactive forms of the Ras protein by chemical modification followed by mass spectrometric peptide mapping

Analytical Biochemistry
S AkashiK Takio


Ras is one of the guanosine triphosphate (GTP) binding proteins that plays a significant role in signaling events of cell growth and differentiation. It can exist in two states: guanosine diphosphate (GDP)-bound from (Ras.GDP; inactive) and GTP-bound form (Ras.GTP; active). This paper discusses the difference in tertiary structure between the active and inactive forms using the combination of chemical modification and mass spectrometry. This difference can be clearly recognized in the presence of a target protein. Raf-1 RBD (Raf-1 Ras-binding domain), as differing glycinamidation of carboxyl groups. It was possible to observe the difference between these two states using several hundred picomoles of sample. While it is true that it is difficult to obtain the whole picture of a protein by the combination of chemical modification and mass spectrometry, it is a promising approach for the characterization of surface structure using very small amounts of sample.

  • References16
  • Citations6


Mentioned in this Paper

Peptide Mapping
Guanosine Diphosphate
Proto-Oncogene Proteins c-raf
Tertiary Protein Structure
Plasma Protein Binding Capacity
Mass Spectrometry
Staphylococcal Protein A
Binding Protein
Protein Serine/Threonine Kinase Activity

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