首页 | 本学科首页   官方微博 | 高级检索  
   检索      


Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic 15N chemical shielding anisotropy tensors
Authors:Ji?í Emmer  Andrea Vavrinská  Vladimír Sychrovský  Ladislav Benda  Zdeněk K?í?  Jaroslav Ko?a  Rolf Boelens  Vladimír Sklená?  Luká? Trantírek
Institution:1. Biology Centre, Academy of Science of the Czech Republic and University of South Bohemia, Brani?ovská 31, 370 05, ?eské Budějovice, Czech Republic
2. Bijvoet Centre for Biomolecular Research, Utrecht University, 3584 CH, Utrecht, The Netherlands
3. Institute of Organic Chemistry and Biochemistry v.v.i., Academy of Science of the Czech Republic, Flemingovo nám. 2, 166 10, Prague, Czech Republic
4. National Centre for Biomolecular Research and CEITEC, Masaryk University, Kamenice 5, 602 00, Brno, Czech Republic
Abstract:Density functional theory was employed to study the influence of O-phosphorylation of serine, threonine, and tyrosine on the amidic 15N chemical shielding anisotropy (CSA) tensor in the context of the complex chemical environments of protein structures. Our results indicate that the amidic 15N CSA tensor has sensitive responses to the introduction of the phosphate group and the phosphorylation-promoted rearrangement of solvent molecules and hydrogen bonding networks in the vicinity of the phosphorylated site. Yet, the calculated 15N CSA tensors in phosphorylated model peptides were in range of values experimentally observed for non-phosphorylated proteins. The extent of the phosphorylation induced changes suggests that the amidic 15N CSA tensor in phosphorylated proteins could be reasonably well approximated with averaged CSA tensor values experimentally determined for non-phosphorylated amino acids in practical NMR applications, where chemical surrounding of the phosphorylated site is not known a priori in majority of cases. Our calculations provide estimates of relative errors to be associated with the averaged CSA tensor values in interpretations of NMR data from phosphorylated proteins.
Keywords:
本文献已被 SpringerLink 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号