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Electrospray Ionization Mass Spectrometry of Genetically and Chemically Modified Bacteriorhodopsins by P. Hufnagel; U. Schweiger; C. Eckerskorn; D. Oesterhelt is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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262 amino acids (2, 3). The protein is processed at the A simple method for the preparation of bacterio-N-terminus in at least three steps by the removal of 7, rhodopsin for mass spectrometry is described, con-10, and 13 amino acids (4), and the final N-terminus sisting of precipitation of the sample, removal of lipforms a pyroglutamate residue (5). The C-terminus is ids by washing the sample, and dissolving it in an shortened by the last aspartic acid which gives the maacidic mixture of organic solvents. Examples demonture protein a length of 248 amino acids and an average strate the method's suitability for the analysis of gemolecular mass of 26,783.6 Da. netically and chemically modified bacteriorhodop-Due to their insolubility, the chemistry and analysis sins. The observed molecular masses are within of membrane proteins are notoriously difficult. For the 0.01% in accordance with the theoretical masses of analysis of posttranslational processing and chemical the wild-type protein and modification products. modifications, as well as for the verification of muta-This allows the detection of modifications accompations introduced using the recently developed system nied by a mass c

Who reads Electrospray Ionization Mass Spectrometry of Genetically and Chemically Modified Bacteriorhodopsins?

Author

P. Hufnagel; U. Schweiger; C. Eckerskorn; D. Oesterhelt

Publisher

Elsevier Science; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 0003-2697)

Published

1996

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)