Protein Chemistry Laboratory - Texas A&M University

Our new website will be coming online late this fall. Our URL will remain the same however. We are looking forward to a better organized, more informative site.

Special AAA

The Protein Chemistry Laboratory offers analysis of DAPA, diaminopimelic acid. This constituent of bacterial cell walls is easily measured on our AminoQuant Amino Acid Analysis system in the low nmol range. Please contact Jinny Johnson (jinny@tamu.edu or 845-2433) for additional information regarding this specific analysis or other amino acid quantitation needs.

DIGE SYSTEM IS INSTALLED

The new DIGE system and robotic spot pickers have been installed in the PCL and training is complete. We are providing quantitative DIGE analysis of protein expression for service. Along with the installation of the new Kratos Axima CFR MALDI-TOF mass spec, we are fully Proteomics Capable for protein identification using Peptide Mass Fingerprinting.

The system is from GE Healthcare and more information can be obtained at their website http://www1.amershambiosciences.com/APTRIX/upp01077.nsf/Content/Products?OpenDocument&parentid=366137&moduleid=165425&zone=Proteomics#content

The PCL will be offering hands-on training workshops in the Spring on the use of this new and exciting technique.

Please check back for updates.

NEW MALDI-TOF MASS SPEC INSTALLED

A Kratos Axima CFR MALDI-TOF mass spectrometer has been installed in the PCL and being used for routine mass measurement as well as Peptide Mass Fingerprinting. It is capable of Post Source Decay which provides MS/MS -like data that is used also for protein identification.

The PCL Web site now has a new hot topics section on the main page, click here to view it.

Check out our News section to learn about new developments at the PCL. Learn about:

- Larry Dangott; Thursday, August 30, 2007, 05:22PM EDT

The Protein Chemistry Laboratory is a core resource facility created and funded under the auspices of the Office of the Vice President for Research of Texas A&M University. The laboratory has been established to support research in protein chemistry and molecular biology in the Texas A&M University System and to provide state-of-the-art instrumentation and technical expertise for the application of modern molecular biological technologies. The PCL is overseen by a committee that meets regularly to discuss issues relevant to the facility's operation. Learn more information about the PCL User Committee.

The laboratory operates as a fee-for-service facility and accepts samples on a first-come-first-served basis from faculty, scientists and students of Texas A&M, other educational institutions and industrial scientists. Main campus users are given preference whenever possible as the facility exists primarily to support of Texas A&M research.

Nature Biotechnology

Enrichment and Analysis of Peptide Subsets Using Fluorous Affinity Tags and Mass Spectrometry

Although mass spectrometry has become a powerful tool for the functional analysis of biological systems, complete proteome characterization cannot yet be achieved. Instead, the sheer complexity of living organisms demands fractionation of cellular extracts to enable more targeted analyses. Here, we introduce the concept of 'fluorous proteomics,' whereby specific peptide subsets from samples of biological origin are tagged with perfluorinated moieties and subsequently enriched by solid-phase extraction over a fluorous-functionalized stationary phase. This approach is extremely selective, yet can readily be tailored to enrich different subsets of peptides. Additionally, this methodology overcomes many of the limitations of traditional bioaffinity-based enrichment strategies, while enabling new affinity enrichment schemes impossible to implement with bioaffinity reagents. The potential of this methodology is demonstrated by the facile enrichment of peptides bearing particular side-chain functionalities or post-translational modifications from tryptic digests of individual proteins as well as whole cell lysates. Click here to read more.

Nature Biotechnology

December 2003; Vol 21, pp 1509-1512

Analyzing antibody specificity with whole proteome microarrays

Although approximately 10,000 antibodies are available from commercial sources, antibody reagents are still unavailable for most proteins1. Furthermore, new applications such as antibody arrays2-5 and monoclonal antibody therapeutics6, 7 have increased the demand for more specific antibodies to reduce cross-reactivity and side effects. An array containing every protein for the relevant organism represents the ideal format for an assay to test antibody specificity, because it allows the simultaneous screening of thousands of proteins for possible cross-reactivity. As an initial test of this approach, we screened 11 polyclonal and monoclonal antibodies to 5,000 different yeast proteins deposited on a glass slide and found that, in addition to recognizing their cognate proteins, the antibodies cross-reacted with other yeast proteins to varying degrees. Some of the interactions of the antibodies with noncognate proteins could be deduced by alignment of the primary amino acid sequences of the antigens and cross-reactive proteins; however, these interactions could not be predicted a priori. Our findings show that proteome array technology has potential to improve antibody design and selection for applications in both medicine and research.