MALDI-TOF Mass Spectrometry in the Protein Biochemistry Lab: From Characterization of Cell Cycle Regulators to the Quest for Novel Antibiotics

doi:https://doi.org/10.1007/978-1-4612-0229-5_6

MALDI-TOF Mass Spectrometry in the Protein Biochemistry Lab: From Characterization of Cell Cycle Regulators to the Quest for Novel Antibiotics

Paul Tempst,Hediye Erdjument‐Bromage,Peter Casteels,Scott Geromanos,Mary Lui,Michael R. Powell+1 more-1996-01-01-Humana Press eBooks

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TL;DRAbstract

For decades, direct covalent analysis was the only way to get the full primary structure of a protein, a tedious task involving several digests and exhaustive analysis [1]. More recently, this process has been accelerated by the use of limited sequence information to assist in cloning of the corresponding genes [2, 3]. Cloned DNA can be readily analyzed and the entire protein primary structure deduced. With a large number of genes sequenced and repositories rapidly expanding [4, 5], partial protein sequences have also allowed, with increasing frequency, matching biological function (or regulation) to a specific database entry [6–8]. The focus of protein sequencing has therefore again shifted to questions of protein associations in the cell. After discovery of one or more components of a functional complex (in signal transduction, cell cycle and differentiation, and vesicle targeting, among other processes), the question typically arises with which other proteins they might interact [9–

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For decades, direct covalent analysis was the only way to get the full primary structure of a protein, a tedious task involving several digests and exhaustive analysis [1]. More recently, this process has been accelerated by the use of limited sequence information to assist in cloning of the corresponding genes [2, 3]. Cloned DNA can be readily analyzed and the entire protein primary structure deduced. With a large number of genes sequenced and repositories rapidly expanding [4, 5], partial protein sequences have also allowed, with increasing frequency, matching biological function (or regulation) to a specific database entry [6–8]. The focus of protein sequencing has therefore again shifted to questions of protein associations in the cell. After discovery of one or more components of a functional complex (in signal transduction, cell cycle and differentiation, and vesicle targeting, among other processes), the question typically arises with which other proteins they might interact [9–

Keywords

Computational biologyCloning (programming)DNA sequencingFunction (biology)Mass spectrometryProteomicsBiologyProtein sequencing

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