Pure shift amide detection in conventional and TROSY-type experiments of 13C,15N-labeled proteins [0.03%]
常规和TROSY型实验中纯位移酰胺检测13C,15N-标记的蛋白质
Jens D Haller,Andrea Bodor,Burkhard Luy
Jens D Haller
Large coupling networks in uniformly 13C,15N-labeled biomolecules induce broad multiplets that even in flexible proteins are frequently not recognized as such. The reason is that given multiplets typically consist of a large number of indiv...
Nicolas Bolik-Coulon,D Flemming Hansen,Lewis E Kay
Nicolas Bolik-Coulon
For the past decade chemical exchange saturation transfer (CEST) experiments have been successfully applied to study exchange processes in biomolecules involving sparsely populated, transiently formed conformers. Initial implementations foc...
Characterization of conformational heterogeneity via higher-dimensionality, proton-detected solid-state NMR [0.03%]
基于高维、 proton检测固态NMR表征构象异质性
Ekaterina Burakova,Suresh K Vasa,Rasmus Linser
Ekaterina Burakova
Site-specific heterogeneity of solid protein samples can be exploited as valuable information to answer biological questions ranging from thermodynamic properties determining fibril formation to protein folding and conformational stability ...
Correction to: Validation of protein backbone structures calculated from NMR angular restraints using Rosetta [0.03%]
题为“使用Rosetta验证由NMR夹角约束计算的蛋白质主链结构”的文章的更正
Joel Lapin,Alexander A Nevzorov
Joel Lapin
Published Erratum
Journal of biomolecular NMR. 2022 Aug;76(4):165. DOI:10.1007/s10858-022-00398-w 2022
Measurement of 1Hα transverse relaxation rates in proteins: application to solvent PREs [0.03%]
蛋白质中氢原子的横向弛豫率测定及其在溶剂PRE中的应用
Yuki Toyama,Atul Kaushik Rangadurai,Lewis E Kay
Yuki Toyama
It has recently been demonstrated that accurate near surface electrostatic potentials can be calculated for proteins from solvent paramagnetic relaxation enhancements (PREs) of amide protons measured using spin labels of similar structures ...
The measurement of binding affinities by NMR chemical shift perturbation [0.03%]
利用核磁共振化学位移变化测定结合亲和力
Billy Hobbs,Jack Drant,Mike P Williamson
Billy Hobbs
We have carried out chemical shift perturbation titrations on three contrasting proteins. The resulting chemical shifts have been analysed to determine the best way to fit the data, and it is concluded that a simultaneous fitting of all raw...
Proton TOCSY NMR relaxation rates quantitate protein side chain mobility in the Pin1 WW domain [0.03%]
proton TOCSY NMR弛豫速率量化了Pin1 WW结构域中的蛋白质侧链流动性
Gaddafi I Danmaliki,Peter M Hwang
Gaddafi I Danmaliki
Protein side chain dynamics play a vital role in many biological processes, but differentiating mobile from rigid side chains remains a technical challenge in structural biology. Solution NMR spectroscopy is ideally suited for this but suff...
Distinct stereospecific effect of chiral tether between a tag and protein on the rigidity of paramagnetic tag [0.03%]
手性连接基团对刚性的顺磁标记物的立体专一性效应
Jia-Liang Chen,Bin Li,Bo Ma et al.
Jia-Liang Chen et al.
Flexibility between the paramagnetic tag and its protein conjugates is a common yet unresolved issue in the applications of paramagnetic NMR spectroscopy in biological systems. The flexibility greatly attenuates the magnetic anisotropy and ...
Metabolic15N labeling of the N-glycosylated immunoglobulin G1 Fc with an engineered Saccharomyces cerevisiae strain [0.03%]
工程酵母菌株合成N-糖基化抗体IgG1 Fc的全相对原子质量氮同位素标记技术研究
Anjali Shenoy,Alexander R Davis,Elijah T Roberts et al.
Anjali Shenoy et al.
The predominant protein expression host for NMR spectroscopy is Escherichia coli, however, it does not synthesize appropriate post-translation modifications required for mammalian protein function and is not ideal for expressing naturally s...
The time-zero HSQC method improves the linear free energy relationship of a polypeptide chain through the accurate measurement of residue-specific equilibrium constants [0.03%]
时间零点HSQC法通过精确测量特定残基平衡常数改善多肽链的线性自由能关系
Seiichiro Hayashi,Daisuke Kohda
Seiichiro Hayashi
EXSY (exchange spectroscopy) NMR provides the residue-specific equilibrium constants, K, and residue-specific kinetic rate constants, k, of a polypeptide chain in a two-state exchange in the slow exchange regime. A linear free energy relati...