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Myoglobin peptides, synthetic

Iwai, K., Fukuoka, S.-I., Fushiki, T., Kido, K., Sengoku, Y., and Semba, T. (1988) Preparation of a verifiable peptide-protein immunogen direction-controlled conjugation of a synthetic fragment of the monitor peptide with myoglobin and application for sequence analysis. Anal. Biochem. 171, 277-282. [Pg.1078]

Since the dispersive properties of helices in what will be taken as the standard sense, now known to be right-handed as in myoglobin, have been the most thoroughly studied and since a case can be made that it is the predominant sense in proteins, this review will focus on the capacity of optical rotatory methods to discern mixtures of this conformation with disordered regions. It will discuss the manner in which theoretical considerations have provided the forms into which rotatory data are currently cast, the calibration of their constants by studies of synthetic polypeptides in known conformation, and then the application of these equations and scales in the structural interpretation of the rotatory dispersion of proteins. This pattern of analysis will undoubtedly undergo refinement and revision as these methods are applied to new species of polypeptide and protein in concert with other means of conformational assignment. In particular, an extension of the spectral range of measurement toward optically active absorption bands in the far ultraviolet can be expected to yield new information about the rotatory power of the peptide bond and thus enhance the interaction of theory and observation that has already proved fruitful. [Pg.403]

Figure 6 Ideal SEC of myoglobin fragments and a mixture of synthetic peptide standards. Column same as Fig. 2. Mobile phase 50 mM KH2P04, containing 500 mM KCI and 8M urea, pH 6.5 flow rate, 0.2mL/min temperature, 26 C. (A) Elution profile of horse heart myoglobin (Mb) and its cyanogen bromide cleavage fragments (I, II, I + II, III) (B) elution profile of horse heart Mb and synthetic peptide standards 1-5 (sequences of standards are shown in Table 1) (C) plot of log,o MW versus elution time of Mb, cyanogen bromide fragments of Mb, and the five synthetic peptide standards. (From Ref. 37.)... Figure 6 Ideal SEC of myoglobin fragments and a mixture of synthetic peptide standards. Column same as Fig. 2. Mobile phase 50 mM KH2P04, containing 500 mM KCI and 8M urea, pH 6.5 flow rate, 0.2mL/min temperature, 26 C. (A) Elution profile of horse heart myoglobin (Mb) and its cyanogen bromide cleavage fragments (I, II, I + II, III) (B) elution profile of horse heart Mb and synthetic peptide standards 1-5 (sequences of standards are shown in Table 1) (C) plot of log,o MW versus elution time of Mb, cyanogen bromide fragments of Mb, and the five synthetic peptide standards. (From Ref. 37.)...

See other pages where Myoglobin peptides, synthetic is mentioned: [Pg.747]    [Pg.60]    [Pg.36]    [Pg.582]    [Pg.851]    [Pg.248]    [Pg.2178]    [Pg.402]    [Pg.64]    [Pg.118]    [Pg.123]    [Pg.2177]    [Pg.561]    [Pg.153]   
See also in sourсe #XX -- [ Pg.35 , Pg.51 ]




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