Two synthetic peptides were completely cleaved by the cis-[Pt(en)(H2O)2]2+ (en is ethylenediamine) complex at pH 2.5 under thermal heating at 60 degrees C in a selective way: only the amide bonds involving the carboxylic group of the methionine residue, i.e., the Met-Z bonds (where the residue Z has a noncoordinating side chain), were hydrolyzed. Under irradiation at 300 nm, the rate constants for these cleavage reactions were approximately doubled, but side reactions occurred. Under microwave irradiation, the rate constants were increased 2-3 times at 60 degrees C and ca. 7 times at 100 degrees C, and no side reactions were detected. Microwave irradiation similarly accelerated the complete and selective cleavage of Met-Z bonds in cytochrome c at 60 degrees C in comparison with this cleavage under thermal heating, again without detected side reactions. The microwave-assisted cleavage of peptides and proteins by the platinum(II) reagent holds promise in proteomics and other biotechnological applications.
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Chapter II. Chemical reagents as selective protein cleavers-Pt(II) complexes Introduction Pt(II) and Pd(II) complexes. Requirements for efficient peptide bond cleavage Pd(II) complexes as selective peptide bond cleavers cis-[Pt(en)(H 2 O) 2 ] 2+ as selective peptide bond cleaver Different selectivities of Pd(II) and Pt(II) reagents as peptide bond cleavers cis-[Pt(en)(H 2 O) 2 ] 2+ versus cyanogen bromide as selective peptide bond cleavers References Chapter III. Platinum(II) complex as an artificial peptidase: selective cleavage of peptides and a protein by cis-[Pt(en)(H 2 O) 2 ] 2+ ion under ultraviolet and microwave irradiation Abstract Introduction Experimental procedures Results and discussion Conclusions and prospects Acknowledgement. References Chapter IV. Pt(II) complexes as selective protein cleavers. General summary and future directions References Chapter V. RNA-protein interactions in the 30S ribosomal subunit Introduction 30S ribosomal subunit-a model system for the study of RNA-protein interactions Ribosomal proteins S4, S7, S8, S15, S17 and S20 RNA-protein interactions in the 30S subunit Dynamics of the r-protein 16S rRNA interaction Directed hydroxyl radical probing in the study of the 30S subunit Chemical reagents in the study of RNA-protein interactions. Footprinting and directed hydroxyl radical probing References iii Chapter VI. Temperature-dependent RNP conformational rearrangements: analysis of binary complexes of primary binding proteins with 16S rRNA
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