A spectroscopic assignment technique for membrane proteins reconstituted in magnetically aligned bicelles [0.03%]
磁性排列双盘中重构的膜蛋白光谱分配技术
Wenxing Tang,Robert W Knox,Alexander A Nevzorov
Wenxing Tang
Oriented-sample NMR (OS-NMR) has emerged as a powerful tool for the structure determination of membrane proteins in their physiological environments. However, the traditional spectroscopic assignment method in OS NMR that uses the "shotgun"...
PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles [0.03%]
PPM：一种用于评估蛋白质构象集合的侧链和主链化学位移预测方法
Da-Wei Li,Rafael Brüschweiler
Da-Wei Li
The combination of the wide availability of protein backbone and side-chain NMR chemical shifts with advances in understanding of their relationship to protein structure makes these parameters useful for the assessment of structural-dynamic...
3D-TROSY-based backbone and ILV-methyl resonance assignments of a 319-residue homodimer from a single protein sample [0.03%]
基于3D-TROSY的同二聚体(单一样品中)完整骨架及ILV甲基共振峰的指认(319残基)
Anna Krejcirikova,Vitali Tugarinov
Anna Krejcirikova
The feasibility of practically complete backbone and ILV methyl chemical shift assignments from a single [U-(2)H,(15)N,(13)C; Ileδ1-{(13)CH(3)}; Leu,Val-{(13)CH(3)/(12)CD(3)}]-labeled protein sample of the truncated form of ligand-free Bst...
Deuterium isotope shifts for backbone ¹H, ¹⁵N and ¹³C nuclei in intrinsically disordered protein α-synuclein [0.03%]
固有无序蛋白α-突触核蛋白主链中1H、15N和13C同位素的氘代同位素效应
Alexander S Maltsev,Jinfa Ying,Ad Bax
Alexander S Maltsev
Intrinsically disordered proteins (IDPs) are abundant in nature and characterization of their potential structural propensities remains a widely pursued but challenging task. Analysis of NMR secondary chemical shifts plays an important role...
Lysine methylation strategies for characterizing protein conformations by NMR [0.03%]
用于NMR表征的赖氨酸甲基化策略蛋白质构象
Sacha Thierry Larda,Michael P Bokoch,Ferenc Evanics et al.
Sacha Thierry Larda et al.
In the presence of formaldehyde and a mild reducing agent, reductive methylation is known to achieve near complete dimethylation of protein amino groups under non-denaturing conditions, in aqueous media. Amino methylation of proteins is emp...
New amino acid residue type identification experiments valid for protonated and deuterated proteins [0.03%]
用于质子化和去垢蛋白的新氨基酸残基类型识别实验有效
David Pantoja-Uceda,Jorge Santoro
David Pantoja-Uceda
Two experiments are presented that yield amino acid type identification of individual residues in a protein by editing the (1)H-(15)N correlations into four different 2D subspectra, each corresponding to a different amino acid type class, a...
CheShift-2 resolves a local inconsistency between two X-ray crystal structures [0.03%]
CheShift-2 解决了两个X射线晶体结构的局部不一致问题
Jorge A Vila,Shih-Che Sue,James S Fraser et al.
Jorge A Vila et al.
Since chemical shifts provide important and relatively accessible information about protein structure in solution, a Web server, CheShift-2, was developed for structure interrogation, based on a quantum mechanics database of (13)C( α ) che...
Optimal degree of protonation for ¹H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency [0.03%]
固态氢谱技术检测随机掺氘蛋白质中亚氨基质子的最佳酸性条件研究：不同MAS频率下的研究
Sam Asami,Kathrin Szekely,Paul Schanda et al.
Sam Asami et al.
The (1)H dipolar network, which is the major obstacle for applying proton detection in the solid-state, can be reduced by deuteration, employing the RAP (Reduced Adjoining Protonation) labeling scheme, which yields random protonation at non...
Kuo-Wei Hung,Yuan-Ming Chang,Chin Yu
Kuo-Wei Hung
PACSY, a relational database management system for protein structure and chemical shift analysis [0.03%]
用于蛋白质结构和化学位移分析的关系型数据库管理系统
Woonghee Lee,Wookyung Yu,Suhkmann Kim et al.
Woonghee Lee et al.
PACSY (Protein structure And Chemical Shift NMR spectroscopY) is a relational database management system that integrates information from the Protein Data Bank, the Biological Magnetic Resonance Data Bank, and the Structural Classification ...