EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 114, Issue 31, Page E6342-E6351, Year 2017
掲載日	2017年8月1日
著者	Gustavo Fuertes / Niccolò Banterle / Kiersten M Ruff / Aritra Chowdhury / Davide Mercadante / Christine Koehler / Michael Kachala / Gemma Estrada Girona / Sigrid Milles / Ankur Mishra / Patrick R Onck / Frauke Gräter / Santiago Esteban-Martín / Rohit V Pappu / Dmitri I Svergun / Edward A Lemke /
PubMed 要旨	Unfolded states of proteins and native states of intrinsically disordered proteins (IDPs) populate heterogeneous conformational ensembles in solution. The average sizes of these heterogeneous ...Unfolded states of proteins and native states of intrinsically disordered proteins (IDPs) populate heterogeneous conformational ensembles in solution. The average sizes of these heterogeneous systems, quantified by the radius of gyration ( ), can be measured by small-angle X-ray scattering (SAXS). Another parameter, the mean dye-to-dye distance ( ) for proteins with fluorescently labeled termini, can be estimated using single-molecule Förster resonance energy transfer (smFRET). A number of studies have reported inconsistencies in inferences drawn from the two sets of measurements for the dimensions of unfolded proteins and IDPs in the absence of chemical denaturants. These differences are typically attributed to the influence of fluorescent labels used in smFRET and to the impact of high concentrations and averaging features of SAXS. By measuring the dimensions of a collection of labeled and unlabeled polypeptides using smFRET and SAXS, we directly assessed the contributions of dyes to the experimental values and For chemically denatured proteins we obtain mutual consistency in our inferences based on and , whereas for IDPs under native conditions, we find substantial deviations. Using computations, we show that discrepant inferences are neither due to methodological shortcomings of specific measurements nor due to artifacts of dyes. Instead, our analysis suggests that chemical heterogeneity in heteropolymeric systems leads to a decoupling between and that is amplified in the absence of denaturants. Therefore, joint assessments of and combined with measurements of polymer shapes should provide a consistent and complete picture of the underlying ensembles.
リンク	Proc Natl Acad Sci U S A / PubMed:28716919 / PubMed Central
手法	SAS (X-ray synchrotron)
構造データ	SASDE23: Labeled nuclear pore complex protein Nup153 (NUL-Alexa488/Alexa594) without denaturant 手法: SAXS/SANS SASDE33: Unlabeled nuclear pore complex protein Nup153 (NUL) with denaturant 手法: SAXS/SANS SASDE43: Labeled nuclear pore complex protein Nup153 (NUL-Alexa488/Alexa594) with denaturant 手法: SAXS/SANS SASDE53: Unlabeled dihydrolipoyllysine-residue succinyltransferase component (BBL) with denaturant 手法: SAXS/SANS SASDE63: Labeled dihydrolipoyllysine-residue succinyltransferase component (BBL-Alexa488/Alexa594) with denaturant 手法: SAXS/SANS SASDE73: Unlabeled cold shock protein (CSP) with denaturant 手法: SAXS/SANS SASDE83: Labeled cold shock protein (CSP-Alexa488/Alexa594) with denaturant 手法: SAXS/SANS SASDE93: Unlabeled thioredoxin (TRX) with denaturant (Thioredoxin 1, TRX) 手法: SAXS/SANS SASDEA3: Labeled thioredoxin (TRX-Alexa488/Alexa594) with denaturant 手法: SAXS/SANS SASDEB3: Unlabeled nuclear pore complex protein Nup98-Nup96 (N98) without denaturant 手法: SAXS/SANS SASDEC3: Unlabeled nucleoporin NSP1 (NSP) without denaturant 手法: SAXS/SANS SASDEH2: Unlabeled nucleoporin NUP49/NSP49 (N49) without denaturant 手法: SAXS/SANS SASDEJ2: Labeled nucleoporin NUP49/NSP49 (N49-Alexa488/Alexa594) without denaturant 手法: SAXS/SANS SASDEK2: Unlabeled nucleoporin NUP49/NSP49 (N49) with denaturant 手法: SAXS/SANS SASDEL2: Labeled nucleoporin NUP49/NSP49 (N49-Alexa488/Alexa594) with denaturant 手法: SAXS/SANS SASDEM2: Unlabeled Nuclear Localization Signal (NLS) from the inner nuclear membrane protein HEH2 without denaturant 手法: SAXS/SANS SASDEN2: Labeled Nuclear Localization Signal from the inner nuclear membrane protein HEH2 (NLS-Alexa488/Alexa594) without denaturant 手法: SAXS/SANS SASDEP2: Unlabeled Nuclear Localization Signal (NLS) from the inner nuclear membrane protein HEH2 with denaturant 手法: SAXS/SANS SASDEQ2: Labeled Nuclear Localization Signal from the inner nuclear membrane protein HEH2 (NLS-Alexa488/Alexa594) with denaturant 手法: SAXS/SANS SASDER2: Unlabeled Importin Beta Binding domain (IBB) from importin subunit alpha-1 without denaturant 手法: SAXS/SANS SASDES2: Labeled Importin Beta Binding Domain (IBB-Alexa488/Alexa594) from importin subunit alpha-1 without denaturant 手法: SAXS/SANS SASDET2: Unlabeled Importin Beta Binding Domain (IBB) from importin subunit alpha-1 with denaturant 手法: SAXS/SANS SASDEU2: Labeled Importin Beta Binding Domain from importin subunit alpha-1 (IBB-Alexa488/Alexa594) with denaturant 手法: SAXS/SANS SASDEV2: Unlabeled nuclear pore complex protein Nup153 (NUS) without denaturant 手法: SAXS/SANS SASDEW2: Labeled nuclear pore complex protein Nup153 (NUS-Alexa488/Alexa594) without denaturant 手法: SAXS/SANS SASDEX2: Unlabeled nuclear pore complex protein Nup153 (NUS) with denaturant 手法: SAXS/SANS SASDEY2: Labeled nuclear pore complex protein Nup153 (NUS-Alexa488/Alexa594) with denaturant 手法: SAXS/SANS SASDEZ2: Unlabeled nuclear pore complex protein Nup153 (NUL) without denaturant 手法: SAXS/SANS
由来	Homo sapiens (ヒト) Escherichia coli (strain k12) (大腸菌) Thermotoga maritima (strain atcc 43589 / msb8 / dsm 3109 / jcm 10099) (バクテリア) Saccharomyces cerevisiae (strain atcc 204508 / s288c) (パン酵母)