NMR Solution Structure of SlyD from <em>Escherichia coli</em>: Spatial Separation of Prolyl Isomerase and Chaperone Function期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

*NMR Solution Structure of SlyD from Escherichia coli: Spatial Separation of Prolyl Isomerase and Chaperone Function*

Authors:	Ulrich Weininger,Caroline Haupt,Kristian Schweimer,Michael Kovermann,Thomas Brü ser,Peter Schaarschmidt,Franz X. Schmid

Affiliation:	¹ Institut für Physik, Fachgruppe Biophysik, Martin-Luther-Universität Halle-Wittenberg, D-06099 Halle (Saale), Germany ² Mitteldeutsches Zentrum für Struktur und Dynamik der Proteine (MZP), Martin-Luther-Universität Halle-Wittenberg, D-06099 Halle (Saale), Germany ³ Lehrstuhl für Biopolymere, Universität Bayreuth, D-95447 Bayreuth, Germany ⁴ Institut für Biologie/Mikrobiologie, Martin-Luther-Universität Halle-Wittenberg, D-06120 Halle (Saale), Germany ⁵ Roche Diagnostics GmbH, Nonnenwald 2, D-82377 Penzberg, Germany ⁶ Laboratorium für Biochemie, Universität Bayreuth, D-95440 Bayreuth, Germany

Abstract:

Keywords:	SlyD, sensitive to lysis D, cytosolic Escherichia coli chaperone SlyD^?, SlyD (1-165 + His tag) RNase T1, ribonuclease T1 RCM-T1, disulfide-reduced and S-carboxymethylated form of a variant of RNase T1 with Ser54 and Pro5 replaced by Gly and Asn, respectively RCM-α-La, disulfide-reduced and S-carboxymethylated form of bovine α-Lactalbumin PPIase, peptidyl-prolyl cis/trans isomerase FKBP12, human FK506 binding protein with 12 kDa MtFKBP17, FKBP with 17 kDa from Methanococcus thermolithotrophicus RDC, residual dipolar coupling NOE, nuclear Overhauser enhancement hNOE, heteronuclear NOE Tat, twin-arginine translocation IF, insert-in-flap HSQC, heteronuclear single-quantum coherence
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