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as natural ligands, palmitic acid, oleic acid among others (Balendiran
et al ., 2000).
Conclusion
Mass spectrometry is indeed a powerful technique that is not limited to
mere mass measurements for small molecules but could also be powerfully
employed for the identification, characterization and structural analysis of
any biomolecule, particularly proteins and their interactions. So far no tech-
nique can parallel the accuracy, rapidity, sensitivity and reliability of MS for
proteomics applications. Bearing in mind that most biological pathways are
governed by proteins and their different temporal isoforms, it is easy to
appreciate the paramount role to be further played by MS in elucidating the
dynamics of various metabolic pathways in the cell. By weighing molecules
and their fragments, we can identify and characterize different biologically
significant entities. Moreover, this can lead to the search for potential bio-
markers related to diseases and aid further unravelling of the fundamental
mechanics of molecular and cellular networks. Furthermore, recent
improvements in MS instrumentation has allowed MS to open an important
new avenue for addressing real biological samples. One major pitfall of the
technique is that molecules to be analyzed must form ions sufficiently sta-
ble under typical MS conditions. For other practical considerations, the
reader is referred to a review by Lubec and Afjehi-Sadat (2007). Overall,
MS is not only important for proteomics but has come of age as a signifi-
cant tool for molecular, cellular and structural biology.
Acknowledgments
We would like to thank Nicholas Harmer (Cambridge University, UK) for
the FGF/FGFR/heparin model structures and Andrew Carter (Medical
Research Council, Cambridge, UK) for the ribosomal structure models. We
also wish to acknowledge helpful comments from Frank Sobott (Oxford
University, UK), Ulrika Nilsson, Therese Redeby, Mohammadreza
Shariatgorji and Gunnar Thorsen (Stockholm University, Sweden).
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