NMR: prediction of molecular alignment from structure using the PALES software. - Wikidata - awgldk - TriplyDB

NMR: prediction of molecular alignment from structure using the PALES software.

NMR: prediction of molecular alignment from structure using the PALES software.

http://www.wikidata.org/entity/Q48590571

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High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein Engineering encodable lanthanide-binding tags into loop regions of proteins Coordination of adjacent domains mediates TACC3-ch-TOG-clathrin assembly and mitotic spindle binding Atomic-level characterization of the ensemble of the Aβ(1-42) monomer in water using unbiased molecular dynamics simulations and spectral algorithms The magic of bicelles lights up membrane protein structure Expanding the utility of NMR restraints with paramagnetic compounds: background and practical aspects Structural basis for sequence specific DNA binding and protein dimerization of HOXA13 Conformational Dynamics and Structural Plasticity Play Critical Roles in the Ubiquitin Recognition of a UIM Domain Structural determinants for Ca2+ and phosphatidylinositol 4,5-bisphosphate binding by the C2A domain of rabphilin-3A The v-myc-induced Q83 Lipocalin Is a Siderocalin p K a Coupling at the Intein Active Site: Implications for the Coordination Mechanism of Protein Splicing with a Conserved Aspartate Molecular basis of the recognition of the ap65-1 gene transcription promoter elements by a Myb protein from the protozoan parasite Trichomonas vaginalis Structure of a Specialized Acyl Carrier Protein Essential for Lipid A Biosynthesis with Very Long-Chain Fatty Acids in Open and Closed Conformations Structure of the RNA claw of the DNA packaging motor of bacteriophage 29 Solution NMR Structure of the Ca2+-bound N-terminal Domain of CaBP7: A REGULATOR OF GOLGI TRAFFICKING Conformational Dynamics of Wild-type Lys-48-linked Diubiquitin in Solution The Structure, Dynamics, and Binding of the LA45 Module Pair of the Low-Density Lipoprotein Receptor Suggest an Important Role for LA4 in Ligand Release Structures of apo- and ssDNA-bound YdbC from Lactococcus lactis uncover the function of protein domain family DUF2128 and expand the single-stranded DNA-binding domain proteome Structural Basis for Ca2+-induced Activation and Dimerization of Estrogen Receptor by Calmodulin Structural analysis of Stc1 provides insights into the coupling of RNAi and chromatin modification Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1 The Structure of the RLIP76 RhoGAP-Ral Binding Domain Dyad: Fixed Position of the Domains Leads to Dual Engagement of Small G Proteins at the Membrane Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings NMR structure of the 5' splice site in the group IIB intron Sc.ai5 --conformational requirements for exon-intron recognition Solution Structure of the Ubiquitin-associated (UBA) Domain of Human Autophagy Receptor NBR1 and Its Interaction with Ubiquitin and Polyubiquitin The Role of Mg(II) in DNA Cleavage Site Recognition in Group II Intron Ribozymes Structural dynamics of the two-component response regulator RstA in recognition of promoter DNA element Structural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric Structure RBFOX and SUP-12 sandwich a G base to cooperatively regulate tissue-specific splicing Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex Structure of the C-Terminal Helical Repeat Domain of Eukaryotic Elongation Factor 2 Kinase Dimer interface of the effector domain of non-structural protein 1 from influenza A virus: an interface with multiple functions Cold-induced changes in the protein ubiquitin Modulation of the disordered conformational ensembles of the p53 transactivation domain by cancer-associated mutations The intrinsic mechanics of B-DNA in solution characterized by NMR Modern Technologies of Solution Nuclear Magnetic Resonance Spectroscopy for Three-dimensional Structure Determination of Proteins Open Avenues for Life Scientists Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media?The dynamic structure of thrombin in solution Structure, dynamics, and Hck interaction of full-length HIV-1 Nef.

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P2860

NMR: prediction of molecular alignment from structure using the PALES software.

http://www.wikidata.org/entity/Q48590571

description

2008 nî lūn-bûn

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2008年の論文

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年學術文章

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2008年學術文章

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name

NMR: prediction of molecular alignment from structure using the PALES software.

@en

NMR: prediction of molecular alignment from structure using the PALES software.

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type

label

NMR: prediction of molecular alignment from structure using the PALES software.

@en

NMR: prediction of molecular alignment from structure using the PALES software.

@nl

prefLabel

NMR: prediction of molecular alignment from structure using the PALES software.

@en

NMR: prediction of molecular alignment from structure using the PALES software.

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Nature Protocols

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NMR: prediction of molecular alignment from structure using the PALES software.

@en

P2860

High-Resolution Nuclear Magnetic Resonance Spectra of Orientated Molecules

Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution

NMR structures of biomolecules using field oriented media and residual dipolar couplings

Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium

Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions

Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution.

Application of dipolar coupling data to the refinement of the solution structure of the sarcin-ricin loop RNA.

A maximum likelihood method for determining D(a)(PQ) and R for sets of dipolar coupling data.

Rapid classification of a protein fold family using a statistical analysis of dipolar couplings.

Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein

P2888

P304

679-690

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scholarly article

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10.1038/NPROT.2008.36

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4

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3

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Markus Zweckstetter

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2008-01-01T00:00:00Z

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5463503

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18388951

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