Protein structure analysis sequence

Protein Structure Prediction, Sequence Analysis and Protein Folding... 

With the development of NMR-based experiments for studying folded proteins, structural analysis of denatured proteins entered a new phase (Wuthrich, 1994 Dobson et al., 1994 Shortle, 1996). Whereas other spectroscopies and hydrodynamic studies give data that correspond to a complex sum of the properties of all residues, NMR spectroscopy extracts information about individual residues. For the first time, local structural features could be directly inferred from the behavior of sets of residues along the sequence. 

A variety of methods are available to detect proteins separated by electrophoresis or to measure the concentration of total protein in a solution. These methods are normally based on the binding of a dye to one of the amino acids in protein, or a color reaction with an amino acid side chain. The most commonly used stains for protein detection on gels are Coomassie Brilliant Blue (98) and silver stain (99,100). These methods detect any protein residues, either in solution or on an electrophoresis gel. Their main requirement is sensitivity, not specificity. New, more sensitive dyes are being developed for the proteomic analysis of protein structure and sequence, for example Ruby Red (101). 

PredictProtein Protein structure analysis Automatic sequence alignment, protein fold recognition, and secondary structure prediction web server 177 www.embl-heidelberg.de/predictprotein/... 

Bioinformatic tools are of increasing importance for the characterization of flavoenzymes. This finding holds for protein sequence and protein structural analysis as well as for gaining insight into the reactivity of the flavin cofactor by combined quantum mechanical and molecular mechanical (QM/MM) simulations (12). 

Gheorge, M. T. and Bergman, T., Deacetylation and internal cleavage of polypeptides for N-terminal sequence analysis, in Methods in Protein Structure Analysis, Atassi, M. Z. and Appella, E., Eds., Plenum Press, New York, 1994. 

Neshich, G., R. C. Togawa, A. L. Mancini, P. R. Kuser, M. E. Yamagishi, G. Pappas, Jr., W. V. Torres, et al. 2003. STING Millennium A web-based suite of programs for comprehensive and simultaneous analysis of protein structure and sequence. Nucleic Acids Res 31 3386-92. 

Pioneering studies by Sanger and co-workers in the period 1945-1955 led to the determination of the amino acid sequence and subsequently the overall structure of insulin from various species (1). This achievement, in conjunction with the earlier work of Banting and Best and of Abel, placed insulin in a unique place among the other proteins. It was one of the first proteins to be recognized as a hormone and thus forced the acceptance of the fact that a protein could be a hormone. It was the first protein whose structure has been elucidated and thus became the vanguard of protein structural analysis and finally, from the discussion that will follow, it becomes apparent that insulin is the first protein to be chemically synthesized. 

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