The working group of Dr. Kurt Hoffmann offers Structural Biology Service

Based on our broad knowledge and experience in structural biology, we offer a complete structural research service, ranging from crystallization screening, x-ray data collection and structure solution to molecular dynamics simulations and experimental validations (e.g. recrystallization, biophysical analysis). If you are interested in ordering our structural biology service for your project, please contact Dr. Kurt Hoffmann (link to Employees/Dr. Kurt Hoffmann)


Mass Spectrometry

As Proteins have the effector function within each cell, the studies about special proteins as well as the whole proteome is necessary to understand biological systems. The number of proteins in a single cell is significant higher than the number of genes, as post-translational modifications and alternative splicing lead to multiple different proteins from a single gene. 

The invention of mass spectrometry and the application of this technology to protein analysis provides a powerful tool in proteomic research and protein studies. The measurement of molecular masses allows scientists to identify proteins and their modifications, to achieve quality assurances after protein purification and to quantitate protein amounts in complex samples.

Protein Identification by MS/MS

For the MS/MS protein identification, each ionised peptide of an enzymatically-digested protein is selected after a first MS analysis was performed. The MS-selected ion is then fragmented by MS/MS-CID (collision induced dissociation) or by MS/MS-ETD (Electron-transfer dissociation), further analysed by a second MS. From all acquired MS/MS-CID or MS/MS-ETD spectra, the sequence information of the respective peptides is derived. These sequence informations are used in a database (Mascot) search to identify the proteins. The MS/MS protein identification is part of our standard mass spectrometry service.

Peptide Mass Fingerprint

In the peptide mass fingerprinting method, the mass spectrum of enzymatically digested protein is acquired. With the mass spectral data a "peptide mass mapping" search in a database is performed. This method is applicable if the sequence of the protein is known and allows for a rapid identification of proteins. As a standard mass spectrometry service the peptide mass fingerprinting can be requested by customers.

Mass determination of intact proteins and peptides In order to check proteins for completeness of sequence, for example as quality control after purification, mass spectrometry can be used to determine the molecular mass of an intact protein or peptide.

Also, the sequence homogenity of a protein solution can be estimated. This information is not always present from peptide mapping experiments.

Another possible use of this technique is the identification of post-translational modifications (PTM) of the protein of interest.

The mass determination of intact proteins and peptides is part of our standard mass spectrometry service.

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