CO-OLIGOMERS OF GLYCINE AND GAMMA-METHYL-L-GLUTAMATE.
Item
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Title
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CO-OLIGOMERS OF GLYCINE AND GAMMA-METHYL-L-GLUTAMATE.
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Identifier
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AAI8423066
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identifier
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8423066
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Creator
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HUCHITAL, MICHAEL ALVIN.
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Contributor
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Fred Naider
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Date
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1984
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Language
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English
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Publisher
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City University of New York.
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Subject
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Chemistry, Biochemistry
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Abstract
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A series of protected co-oligopeptides consisting of (gamma)-methyl-L-glutamate and one glycine were synthesized from the di- through heptapeptides. Glycine was placed at each position of the oligopeptide backbone except the carboxyl terminus. Determination of the effect of such a substitution on the conformation of the glutamate backbone was achieved via circular dichroism in both trifluoroethanol and hexafluoroisopropanol.;Synthesis was achieved via the mixed carbonic-carboxylic anhydride coupling procedure. Purity for all peptides was equal to or greater than 97% as determined by normal phase HPLC.;Glycine insertion at the amine terminus of the heptapeptide resulted in C.D. spectra indicative of a slight decrease of helicity as compared to the homo-heptamer in trifluoroethanol. Progressive movement of glycine to the interior positions of the heptapeptide resulted in a gradual loss of C.D. patterns associated with peptides in an (alpha)-helical array. Glycine positioned at the fourth position resulted in a complete loss of helicity. Further movement past this internal position toward the carboxyl terminus marked the return of C.D. patterns that indicated some helical character. Virtually all oligopeptides were disordered in trifluoroethanol and hexafluoroisopropanol. Polarimetric analysis in trifluoroethanol and hexafluoroisopropanol supports the conclusions of the C.D. studies.;HPLC on normal phase silica suggests a dependence of mobility of the compounds on their individual conformational distribution.
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Type
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dissertation
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Source
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PQT Legacy CUNY.xlsx
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degree
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Ph.D.
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Program
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Biochemistry
