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Current methods in structural proteomics and its applications in biological sciences

View Article: PubMed Central

ABSTRACT

A broad working definition of structural proteomics (SP) is that it is the process of the high-throughput characterization of the three-dimensional structures of biological macromolecules. Recently, the process for protein structure determination has become highly automated and SP platforms have been established around the globe, utilizing X-ray crystallography as a tool. Although protein structures often provide clues about the biological function of a target, once the three-dimensional structures have been determined, bioinformatics and proteomics-driven strategies can be employed to derive their biological activities and physiological roles. This article reviews the current status of SP methods for the structure determination pipeline, including target selection, isolation, expression, purification, crystallization, diffraction data collection, structure solution, refinement and functional annotation.

No MeSH data available.


Process involved in SP using X-ray crystallography
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Fig1: Process involved in SP using X-ray crystallography

Mentions: When protein structure analysis was first established in the late 1960s and the X-ray structures of myoglobin and hemoglobin were determined, the development of such a high-throughput (HT) infrastructure for protein structure analysis would have seemed like an impossible dream. The remarkable success and technological advancements since then have had a tremendous impact on throughput in protein structure determination and all stages of the pipeline have become more or less automated (Fig. 1). Currently, SP initiatives are generating protein structures at an unprecedented rate and have resulted in an exponential growth in the number of protein structures deposited in the Protein Data Bank (Fig. 2: 65979 PDB entries, as of August 2011). However, the number of solved protein structures in the PDB represents only a small proportion of the theoretical number of proteins encoded by genomic sequences.Fig. 1


Current methods in structural proteomics and its applications in biological sciences
Process involved in SP using X-ray crystallography
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3376864&req=5

Fig1: Process involved in SP using X-ray crystallography
Mentions: When protein structure analysis was first established in the late 1960s and the X-ray structures of myoglobin and hemoglobin were determined, the development of such a high-throughput (HT) infrastructure for protein structure analysis would have seemed like an impossible dream. The remarkable success and technological advancements since then have had a tremendous impact on throughput in protein structure determination and all stages of the pipeline have become more or less automated (Fig. 1). Currently, SP initiatives are generating protein structures at an unprecedented rate and have resulted in an exponential growth in the number of protein structures deposited in the Protein Data Bank (Fig. 2: 65979 PDB entries, as of August 2011). However, the number of solved protein structures in the PDB represents only a small proportion of the theoretical number of proteins encoded by genomic sequences.Fig. 1

View Article: PubMed Central

ABSTRACT

A broad working definition of structural proteomics (SP) is that it is the process of the high-throughput characterization of the three-dimensional structures of biological macromolecules. Recently, the process for protein structure determination has become highly automated and SP platforms have been established around the globe, utilizing X-ray crystallography as a tool. Although protein structures often provide clues about the biological function of a target, once the three-dimensional structures have been determined, bioinformatics and proteomics-driven strategies can be employed to derive their biological activities and physiological roles. This article reviews the current status of SP methods for the structure determination pipeline, including target selection, isolation, expression, purification, crystallization, diffraction data collection, structure solution, refinement and functional annotation.

No MeSH data available.