Protein metrical analyses

Iteble 23.5. Metrical analysis of hydrogen bonds between water molecules and protein functional groups. The data are taken from the 15 protein crystal structures with water positions located, see Tkble 19.1, Part III, and [596]. Compare with Fig. 23.5 with somewhat different sampling... 

Cadene, M., Chait, B. T. (2000). A robust, detei ent-fiiendly method for mass spectro-metric analysis of integral membrane proteins. Analytical Chemistry, 72(22), 5655-5658. 

To overcome problems with automation and recovery, ZipTip sampling has been developed, which is best regarded as miniaturized and simplified SPE equipment. It is frequently used in the field of proteomics, mostly as the last sample preparation step. Sample amount is only a few (3-30) p,l, containing less than a picomole protein digest. Commonly it is used to remove salts and detergents from the sample, e.g., after tryptic digest, just before mass spectro-metric analysis. 

Hepner, E, Cszasar, E., Roitinger, E., and Lubec, G. (2005) Mass spectro-metrical analysis of recombinant human growth hormone (Genotropin ) reveals amino acid substitutions in 2% of the expressed protein. Proteome Science, 3,1. 

In this chapter, we will survey the kinds of solid supports (substrates) and surface chemistries currently used in the creation of nucleic acid and protein microarrays. Which are the best supports and methods of attachment for nucleic acids or proteins Does it make sense to use the same attachment chemistry or substrate format for these biomolecules In order to begin to understand these kinds of questions, it is important to briefly review how such biomolecules were attached in the past to other solid supports such as affinity chromatography media, membranes, and enzyme-linked immxm-osorbent assay (ELISA) microtiter plates. However, the microarray substrate does not share certain unique properties and metrics with its predecessors. Principal among these are printing, spot morphology, and image analysis they are the subjects of subsequent chapters. 

In the following, the geometrical data obtained from a number of protein crystal structures determined at high resolution are analyzed in terms of hydrogen-bonding patterns, and then the data are compared metrically. This procedure and the data analysis are taken mainly from a review of Baker and Hubbard [596], who considered in detail the protein structures listed in Thble 19.1. 

Setchell, K. D. R. and Welsh, M. B., High-performance liquid chromatographic analysis of ph)4oestrogens in soy protein preparations with ultraviolet, electrochemical and TS mass spectro-metric detection, J. Chromatogr., 386, 315-323, 1987. 

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