A Minimalist Approach to Cys-X2-Cys/Zn2+ in Proteins.
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Accession number;00A0163487
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| Title;A Minimalist Approach to Cys-X2-Cys/Zn2+ in Proteins. |
| Author;
YAMAMURA TAKESHI
(Sci. Univ. of Tokyo, Fac. of Sci.)
KOBAYASHI KATSUAKI
(Sci. Univ. of Tokyo, Fac. of Sci.)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.14th;NO.;PAGE.56-57(1999)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Synthetic routes to the minimal peptide models of the zinc binding sites of zinc proteins, Cys-X2-Cys/M2+, are reported. The conformational behavior of [(Boc-Cys-Pro-Leu-Cys-X)Zn(L)2,3], where X=OMe and Gly-Ala-OMe, L=DMF, in DMF-d7 and CDCl3, as well as the substitution reactivity were studied by 1H NMR and EXAFS with respect to the local dynamics of Cys-X2-Cys/Zn2+ and Cys-X2-Cys-Y2/Zn2+ in proteins. Our experiments on these compounds suggested that the conformation of Cys-X2-Cys/Zn2+ is very sensitive to van der Waals contact or coordination of some ligand groups in polar carbonyl environments. This is in contrast to the results obtained from less polar solvents such as CDCl3, where conformations are easily fixed. On the other hand, the elongation of the peptide sequence from four to six induces an extended conformational deviation under carbonyl environment, probably due to increased combinatorial probability of hydrogen bonding linkage. (author abst.) |
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