Complete 13C assignments for recombinant Cu(I) rusticyanin prediction of secondary structure from patterns of chemical shifts

FEBS Letters

Jane Dyson, H.¹  Toy-Palmer, Anna¹  Prytulla, Stefan¹ 

[1] The Scripps Research Institute, 10666 North Torrey Pines Road, La Jolla, CA 92037, USA

关键词: Rusticyanin;    Type 1 copper protein;    Secondary structure;   

DOI  :  10.1016/0014-5793(95)00423-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Complete resonance assignments for the ¹³C spectrum of reduced (Cu(I)) rusticyanin have been made using ¹³C,¹⁵N doubly labeled recombinant material. The reported assignments include those for the carboxyl and carbon l carbon atoms and protonated aromatic ring carbons, and were obtained using a variety of 2- and 3D inverse-detected NMR experiments, including ¹³C,¹⁵N,¹H triple resonance experiments and HCCH-COSY and -TOCSY. Backbone carbonyl assignments were obtained using 3D HNCO and HCACO spectra, and modified versions of 2D H(CA)CO and HMBC spectra were used to obtain side-chain carboxyl carbon and methionine ϵ-methyl carbon assignments, respectively. A comparison of the ¹³C^α, ¹³C^β and ¹³CO chemical shifts with published ‘random coil’ values confirms the conclusion reached from a consideration of the ³ J _HNα coupling constants and the pattern of sequential NOEs, that the protein consists largely of β-structure.

【 授权许可】

Unknown