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Titlebook: Methods in Proteome and Protein Analysis; Roza Maria Kamp,Juan J. Calvete,Theodora Choli-Pap Book 2004 Springer-Verlag Berlin Heidelberg 2

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https://doi.org/10.1007/978-3-662-08722-0Amino acid; In silico; Proteomics; amino acid analysis; bioinformatics; genome; membrane proteins; protein
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Book 2004relation study using optical biosensors of microcolorimetrical techniques; structural proteomics as NMR or fluorescence polarization study; the classification and prediction of structure or functional sites; in silico analysis of proteins and proteomes; increasing throughput and data quality for proteomics..
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Mobility Studies in Proteins by 15N Nuclear Magnetic Resonance: Rusticyanin as an Example,ear NMR study on rusticyanin (Rc). Rc possesses a very high redox potential and is very stable at low pH values. Our study reveals that Rc is also very rigid and highly hydrophobic. The present study strongly indicates that both thermodynamic and mobility properties of Rc are correlated.
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,Analysis of Protein—Protein Interactions in Complex Biological Samples by MALDI TOF MS. Feasibilitywith each other, and with their main ligands, is an issue of fundamental interest for the comprehension of cellular functions (Alberts, 1998), as well as for the efficient application of most biomedical or biotechnological strategies based on them.
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A New Edman-Type Reagent for High Sensitive Protein Sequencing,ne interface are being optimized. The combination of the new coupling reagent with the Chip Sequencer and detection in a GC system makes amino acid sequencing in the low femtomole range feasible and will largely support any future proteome research. A sequencer combining these features will be commercially available in spring 2004.
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