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Chapter 2 : Introduction to Protein Analysis

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Abstract:

There are multiple sources of variation in individual proteins and in the proteome. Posttranslational modifications of the primary translation products of mRNAs potentially lead to large numbers of structural variants of individual gene products. As proteins undergo extracellular and intracellular degradation, a complex array of peptides is generated, quite possibly even more complex than the original set of proteins. Peptide splicing has recently been identified as another mechanism that may increase peptide diversity. In order to understand many pathophysiological processes, such as prion diseases, amyloidosis, hemoglobinopathies, and apoptotic processes, simple primary sequence analysis of proteins is inadequate. Two additional challenges to protein analysis that are nearly as great as structural diversity are (i) the dynamic nature of protein concentration and (ii) the wide range of protein concentrations. Unlike the case for nucleic acids, there is no simple method for amplification of the concentration of proteins. Most methods for protein analysis have a practical analytical concentration range of only about 100to 10,000-fold, and the highest-resolution separation methods for protein analysis, such as two-dimensional gel electrophoresis, have the capability of resolving only up to a few thousand components in a single analysis.

Citation: Hortin G, Remaley A. 2006. Introduction to Protein Analysis, p 4-6. In Detrick B, Hamilton R, Folds J (ed), Manual of Molecular and Clinical Laboratory Immunology, 7th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815905.ch2

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High-Performance Liquid Chromatography
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Reactive Oxygen Species
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Figures

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FIGURE 1

Molecular diversity: increasing complexity through steps in expression of genetic information and common methods of analysis. 2-D PAGE, two-dimensional polyacrylamide gel electrophoresis; HPLC, high-performance liquid chromatography; MALDI TOF MS, matrix-assisted laser desorption ionization-time of flight mass spectrometry.

Citation: Hortin G, Remaley A. 2006. Introduction to Protein Analysis, p 4-6. In Detrick B, Hamilton R, Folds J (ed), Manual of Molecular and Clinical Laboratory Immunology, 7th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815905.ch2
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References

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1. Anderson, N. L., and , N. G. Anderson. 2002. The human plasma proteome: history, character, and diagnostic prospects. Mol. Cell. Proteomics 1:845-867.
2. Anderson, N. L.,, M. Polanski,, R. Pieper,, T. Gatlin,, R. S. Tirumalai,, T. P. Conrads,, T. D. Veenstra,, J. N. Adkins,, J. G. Pounds,, R. Fagan, and , A. Lobley. 2004. The human plasma proteome: a nonredundant list developed by combination of four separate sources. Mol. Cell. Proteomics 3:311-326.
3. De Hoog, C. L., and , M. Mann. 2004. Proteomics. Annu. Rev. Genomics Hum. Genet. 5:267293.
4. Engelhard, V. H. 1994. Structure of peptides associated with class I and class II molecules. Annu. Rev. Immunol. 12:181-207.
5. Engelhard, V. H.,, A. G. Brickner, and , A. L. Zarling. 2002. Insights into antigen processing gained by direct analysis of the naturally processed class I MHC associated peptide repertoire. Mol. Immunol. 39:127137.
6. Hanada, K.,, J. W. Yewdell, and , J. C. Yang. 2004. Immune recognition of a human renal cancer antigen through posttranslational protein splicing. Nature 427:252256.
7. International Human Genome Sequencing Consortium. 2004. Finishing the euchromatic sequence of the human genome. Nature 431:931945.
8. Li, Z.,, C. J. Woo,, M. D. Iglesias-Ussel,, D. Ronai, and , M. D. Scharff. 2004. The generation of antibody diversity through somatic hypermutation and class switch recombination. Genes Dev. 18:111.
9. Pieper, R.,, C. L. Gatlin,, A. J. Makusky,, P. S. Russo,, C. R. Schatz,, S. S. Miller,, Q. Su,, A. M. McGrath,, M. A. Estock,, P. P. Parmar,, M. Zhao,, S. T. Huang,, J. Zhou,, E. Wang,, R. Esquer-Blasco,, N. L. Anderson,, J. Taylor, and , S. Steiner. 2003. The human serum proteome: display of nearly 3700 chromatographically separated protein spots on two-dimensional electrophoresis gels and identification of 325 distinct proteins. Proteomics 3:13451364.
10. Rudolf, R.,, P. Schulz-Knappe,, M. Schrader,, L. Standker,, M. Jurgens,, H. Tammen, and , W.-G. Forssmann. 1999. Composition of the peptide fraction in human blood plasma: database of circulating human peptides. J. Chromatogr. B 726:2535.
11. Seo, J., and , K. J. Lee. 2004. Post-translational modifications and their biological functions: proteomic analysis and systematic approaches. J. Biochem. Mol. Biol. 37:3544.
12. Veenstra, T. D. 2003. Proteome analysis of posttranslational modifications. Adv. Prot. Chem. 65:161194.

Tables

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TABLE 1

Elements of protein diversity

Citation: Hortin G, Remaley A. 2006. Introduction to Protein Analysis, p 4-6. In Detrick B, Hamilton R, Folds J (ed), Manual of Molecular and Clinical Laboratory Immunology, 7th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815905.ch2

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