Backbone 1H, 15N and 13C resonance assignments of the 27kDa fluorescent protein mCherry

被引：0
作者：
Marco Sette
Laura Anne Johnson
Ralph Jimenez
Frans A.A. Mulder
机构：
[1] University of Rome “Tor Vergata”,Department of Chemical Sciences and Technology
[2] Sorbonne Paris Cité,CSPBAT Laboratory
[3] University of Paris 13,Department of Biochemistry
[4] UMR 7244,Department of Chemistry
[5] CNRS,Interdisciplinary Nanoscience Center iNANO and Department of Chemistry
[6] University of Colorado,Institute of Biochemistry
[7] JILA,undefined
[8] University of Colorado,undefined
[9] and NIST,undefined
[10] University of Colorado,undefined
[11] University of Aarhus,undefined
[12] Johannes Kepler Universität Linz,undefined
来源：
Biomolecular NMR Assignments | 2023年 / 17卷
关键词：
mCherry; Red fluorescent protein; Protein engineering; Photostability; Chemical shift;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
mCherry is one of the most successfully applied monomeric red fluorescent proteins (RFPs) for in vivo and in vitro imaging. However, questions pertaining to the photostability of the RFPs remain and rational further engineering of their photostability requires information about the fluorescence quenching mechanism in solution. To this end, NMR spectroscopic investigations might be helpful, and we present the near-complete backbone NMR chemical shift assignment to aid in this pursuit.
引用
收藏
页码：243 / 247
页数：4
相关论文
共 28 条
[1]  
Delaglio F(1995)NMRPipe: a multidimensional spectral processing system based on UNIX pipes J Biomol NMR 6 277-293
[2]  
Grzesiek S(2004)STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins Nucleic Acids Res 32 W500-W502
[3]  
Vuister GW(2015)NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy Bioinforma Oxf Engl 31 1325-1327
[4]  
Zhu G(2021)CheSPI: chemical shift secondary structure population inference J Biomol NMR 75 273-291
[5]  
Pfeifer J(2004)Improved monomeric red, orange and yellow fluorescent proteins derived from Nat Biotechnol 22 1567-1572
[6]  
Bax A(2009). red fluorescent protein J Biomol NMR 44 213-223
[7]  
Heinig M(2006)TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts Biochemistry 45 9639-9647
[8]  
Frishman D(undefined)Novel chromophores and buried charges control color in mFruits undefined undefined undefined-undefined
[9]  
Lee W(undefined)undefined undefined undefined undefined-undefined
[10]  
Tonelli M(undefined)undefined undefined undefined undefined-undefined
123