Improved technologies now routinely provide protein NMR structures useful for molecular replacement.
Improved technologies now routinely provide protein NMR structures useful for molecular replacement.
Improved technologies now routinely provide protein NMR structures useful for molecular replacement.
Structure. 2011 Jun 8;19(6):757-66
Authors: Mao B, Guan R, Montelione GT
Molecular replacement (MR) is widely used for addressing the phase problem in X-ray crystallography. Historically, crystallographers have had limited success using NMR structures as MR search models. Here, we report a comprehensive investigation of the utility of protein NMR...
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06-08-2011 11:30 AM
[NMR paper] NMR chemical shift and relaxation measurements provide evidence for the coupled foldi
NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain.
Related Articles NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain.
Nucleic Acids Res. 2005;33(7):2061-77
Authors: Vise PD, Baral B, Latos AJ, Daughdrill GW
The interaction between the acidic transactivation domain of the human tumor suppressor protein p53 (p53TAD) and the 70 kDa subunit of human replication protein A (hRPA70)...
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11-24-2010 11:14 PM
[NMR paper] NMR-detected hydrogen exchange and molecular dynamics simulations provide structural
NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126.
Related Articles NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126.
Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14790-5
Authors: Kuwata K, Matumoto T, Cheng H, Nagayama K, James TL, Roder H
PrP106-126, a peptide corresponding to residues 107-127 of the human prion protein, induces neuronal cell...
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11-24-2010 09:16 PM
[NMR paper] Binding of copper(II) ions to the polyproline II helices of PEVK modules of the giant
Binding of copper(II) ions to the polyproline II helices of PEVK modules of the giant elastic protein titin as revealed by ESI-MS, CD, and NMR.
Related Articles Binding of copper(II) ions to the polyproline II helices of PEVK modules of the giant elastic protein titin as revealed by ESI-MS, CD, and NMR.
Biopolymers. 2003 Oct;70(3):297-309
Authors: Ma K, Wang K
Titin, a family of giant elastic proteins, constitutes an elastic sarcomere matrix in striated muscle. In the I-band region of the sarcomere, the titin PEVK segment acts as a molecular...
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11-24-2010 09:16 PM
Solid-state NMR and SAXS studies provide a structural basis for the activation of alp
Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.
Related Articles Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.
Nat Struct Mol Biol. 2010 Aug 29;
Authors: Jehle S, Rajagopal P, Bardiaux B, Markovic S, Kühne R, Stout JR, Higman VA, Klevit RE, van Rossum BJ, Oschkinat H
The small heat shock protein alphaB-crystallin (alphaB) contributes to cellular protection against stress. For decades, high-resolution structural studies on...
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08-31-2010 09:42 PM
Constraining Binding Hot Spots: NMR and Molecular Dynamics Simulations Provide a Stru
Constraining Binding Hot Spots: NMR and Molecular Dynamics Simulations Provide a Structural Explanation for Enthalpy−Entropy Compensation in SH2−Ligand Binding
Joshua M. Ward<sup>†</sup>, Nina M. Gorenstein<sup>†</sup>, Jianhua Tian<sup>‡</sup>, Stephen F. Martin<sup>‡</sup> and Carol Beth Post*<sup>†</sup>
Department of Medicinal Chemistry, Markey Center for Structural Biology, and Purdue Cancer Center, Purdue University, West Lafayette, Indiana 47907, and Department of Chemistry and Biochemistry and The Institute of Cellular and Molecular Biology, The University of Texas,...
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08-14-2010 05:56 AM
KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies
KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies
Naohiro Kobayashi, Junji Iwahara, Seizo Koshiba, Tadashi Tomizawa, Naoya Tochio, Peter Güntert, Takanori Kigawa and Shigeyuki Yokoyama
Journal of Biomolecular NMR; 2007; 39(1) pp 31 - 52
Abstract:
The recent expansion of structural genomics has increased the demands for quick and accurate protein structure determination by NMR spectroscopy. The conventional strategy without an automated protocol can no longer satisfy the needs of high-throughput...
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