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Structural studies of a synthetic peptide derived from the carboxyl-terminal domain of RNA polymerase II by Perseveranda M. Cagas; Jeffry L. Corden is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The conformation of the repeating heptapeptide unit of the carboxyl‐terminal domain of RNA Polymerase II, Y^1^S^2^P^3^T^4^S^5^P^6^S^7^ has been examined using nuclear magnetic resonance spectroscopy and circular dichroism. Nuclear Overhauser effects and CD spectra for the synthetic 56‐residue peptide H~2~N‐(S^2^P^3^T^4^S^5^P^6^S^7^Y^l^)~8~‐COOH in water indicate that the peptide is largely unordered. A small population of folded molecules is observed to contain β‐turns located at Ser^2^‐Pro^3^‐Thr^4^‐Ser^5^ (SPTS) and Ser^5^‐Pro^6^‐Ser^7^‐Tyr^1^ (SPSY). CD and NMR results in 90% TFE also indicate an equilibrium population of structures, but the fraction of turns is higher. Similarities of nuclear Overhauser effects in water and in 90% TFE suggest that the structures in TFE are biologically relevant. Based on these observations, the average structure of a single conformer of the heptapeptide repeat in 90% TFE was obtained by a distance geometry‐simulated annealing method, using distance restraints extracted from nuclear Overhauser data. NMR spectra of the 56‐mer show signals corresponding to only one repeat indicating that each repeat is in an identical environment. Thus

Who reads Structural studies of a synthetic peptide derived from the carboxyl-terminal domain of RNA polymerase II?

Author

Perseveranda M. Cagas; Jeffry L. Corden

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

1995

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)