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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The Functional Interaction Trap: A Novel Strategy to Study Specific Protein-Protein Interactions,standing a host of cellular processes. Whether it is an enzyme modifying its substrate, the assembly of subunits of a multiprotein complex, the recognition and binding of a specific ligand, or the polymerization of monomeric subunits such as those of actin, protein-protein interactions are essential

fidelity

GLOOM

Accelerator Mass Spectrometry in Protein Analysis, discovered in the nineteenth century and quantified by gravimetric mass determination of chemical precipitates. Finer fractionations and scales led to quantitation of increasingly less common proteins, but the method has obvious limits. Some proteins, enzymes, are quantified by their ., measured as

Mercantile

The Use of Microcalorimetric Techniques to Study the Structure and Function of the Transferrin Rececurrently no vaccine to prevent serogroup B meningococcal disease. The proteins which form the transferrin receptor of . are promising candidates for inclusion in such a vaccine (Gorringe et al. 1995). The receptor consists of two types of subunits, transferrin-binding protein A and B (TbpA and B),

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The Quantitative Advantages of an Internal Standard in Multiplexing 2D Electrophoresis,n a single gel (Gorg et al. 2000). This tool separates proteins by pI (isoelectric point) and molecular weight producing a pattern of spots on an SDS-PAGE (polyacrylamide gel electrophoresis) gel, which can be visualised via a range of staining and labelling systems. Protein spot patterns can be com

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Genetic Engineering of Bacterial and Eukaryotic Ribosomal Proteins for Investigation on Elongation ngation arrest of the nascent polypeptides and cell differentiation. These objectives have been approached by: (1) engineering the L4 bacterial ribosomal protein, which has been shown by crystallographic data to be a candidate molecule for controlling the nascent polypeptides before their emerge fro

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MALDI-MS Analysis of Peptides Modified with Photolabile Arylazido Groups,e subjected to MALDI-MS analysis in a variety of matrices. As a standard MALDI-MS employs a UV laser (337 nm), we investigated conditions that would allow detection of the intact molecule ions for these modified peptides. When using a-cyano-4-hydroxycinnamic acid (ACHC) or 2,5 dihydroxybenzoic acid

HERE

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978-3-642-05779-3Springer-Verlag Berlin Heidelberg 2004