Protein comparison

Villoing A, Ridhoir M, Cinquin B, Erard M, Alvarez L, Vallverdu G, Pemot P, Grailhe R, Merola F, Pasquier H (2008) Complex fluorescence of the cyan fluorescent protein comparisons with the FU48D variant and consequences for quantitative cell imaging. Biochemistry 47 12483-12492... 

Model proteins Comparison of the separation on SMC (CIM ), UNO, Mono Q and Sartobind columns Anion Exchange disks [92]... 

Fig. 3. Schematic view of pairs of protein comparisons. Each protein is represented as a horizontal line, with the domains marked as boxes or ovals. Three pairs of proteins are shown, with domains that are related between the pair shaded gray, and domains that are unique to one of the sequences shown unshaded. The region of pairwise similarity is boxed within dashed lines. See text for a fuller explanation.

EAST A EAST ALL (a programme for fast protein comparison or fast... 

Levison PR. Large-scale ion exchange column chromatography of proteins Comparison of different formats. Journal of Chromatography B 2003 790 17-33. 

Mangino, M. E. and Brunner, J. R. 1977B. Compositional homology of membrane-protein systems and membrane-associated proteins Comparison with milk fat globule membrane and membrane -derived xanthine oxidase. J. Dairy Sci. 60, 1208-1216. 

Graham, A K, Herrington, C S, and McGee JO D (1991) Sensitivity and specificity of monoclonal antibodies to human papillomavirus Type 16 Capsid protein-comparison with simultaneous viral detection by nonisotopic in situ hybridization J Clin Pathol 44,96-101... 

Comparing and overlapping two protein structures quantitatively remain an active area of development in structural biochemistry. Methods for protein comparison generally rely on a fast full search of protein structure database. Some of these methods that are available over the Internet are listed in Table 15.1. 

Daizadch I, Gehlen JN, Stuchebrukhof AA. Calculation of electronic tunneling matrix element in proteins comparison of exact and approximate one-electron methods for Ru-modified azurin. J Chem Phys 1997 106 5658-66. 

Loewenthal, R., Sancho, J., Reinikainen, T. and Fersht, A R. (1993) Long-range surface charge-charge interactions in proteins comparison of experimental results with calculations from a theoretical method. J. Mol. Biol., 232, 574-583. 

Yvon, M., Beucher, S., Scanff, P.,Thirouin, S., and Pelissier, J. P. (1992), In vitro simulation of gastric digestion of milk proteins Comparison between in vitro and in vivo data, J. Agric. Food Chem., 40, 239-244. 

Price et al. (5) measured the retention of zinc and other minor elements in studies in which the major variables were source and level of dietary protein. Comparison of protein sources from plant and mixed sources indicated that the apparent absorption was somevJhat lower from the diets with only plant proteins than that from mixed sources. A lower level of protein (25 g/day) caused a lower retention of zinc than the moderate protein (46 g/day) diet, although conclusions were complicated because of other variables. 

Chen, L., and Roberts, M.F., 2000, Overexpression, purification, and analysis of complementation behavior of E. coli Suhb protein Comparison with bacterial and archaeal inositol monophosphatases. Biochemistry 39 4145 4153. 

To analyze the subtle specific structural features of thermophilic archaeal proteins, comparisons with closely related mesophilic proteins are necessary. Since the Crenarchaeota comprise exclusively thermophilic strains, respective comparisons are only possible with proteins from Euryarchaeota. Structural comparisons between thermophilic archaeal proteins and mesophilic bacterial or eucaryal proteins are unlikely to be useful because of the large evolutionary distance between different domains, which blur the thermoadaptive features. 

Figure 5-7 Rapid protein electrophoresis of serum protein comparison with scanning densitometry profiles obtained from CAE and AGE electrophoresis. Panel A—normal serum, Panel B—patient serum containing a large M-protein Panel C—patient serum containing a small monoclonal protein. The arrows indicate the position of the monoclonal proteins.

A stable isotope dilution assay using mass spectrometry to measure insulin, proinsulin, and C-peptide has been developed. The difference in mass among the three analytes allows specific measurement of each protein. Comparison of patient samples revealed that most, but not all, results were higher by immunoassay than mass spectrometry. Thus immunoassays may overestimate insulin, particularly at low concentrations. The high protein concentration in the serum requires extraction of proteins (e.g., by immunoaffinity) and purification by high-performance liquid chromatography (HPLC) before quantification by mass spectrometry. This method is not suitable for routine laboratory analysis. 

P. Dauber-Osguthorpe, D. J. Osguthorpe, P. S. Stem and J. Moult, Low frequency motion in proteins comparison of normal mode and molecular dynamics of streptomyces griseus protease A, J. Comput. Phys., 151(1), 169-189 (1999). 

W9. Wright, G. L., Farrell, K. B., and Roberts, D. B., An evaluation of gradient acrylamide gel electrophoresis and acrylamide gel isoelectric focusing for the primary separation of complex mixtures of proteins Comparison of one- and two-dimensional analytical procedures. Biochim. Biophys. Acta 295, 396-411 (1973). 

Christensen, I. T. Jorgensen, F. S. (1997). Molecular mechanics calculations of proteins. Comparison of different energy minimization strategies. / Biomol Struct Dyn 15(3), 473-88. 

Kovacs GG, Head MW, Hegy I, et al. Immunohistochemistry for the prion protein Comparison of different monoclonal antibodies in human prior disease subtypes. Brain Pathol. 2002 12 1-11. 

---