Protein stays stable without its charges - The Biological SCENE
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The Biological SCENE
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Protein stays stable without its charges
The Biological SCENE
... methionine, and tryptophan, respectively. After expressing their mutant protein in Escherichia coli, the researchers tested its solubility and stability and assessed the protein's structure with circular dichroism and nuclear magnetic resonance ...
Protein stays stable without its charges - The Biological SCENE
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07-25-2016 04:26 PM
â??CON-CONâ?? assignment strategy for highly flexible intrinsically disordered proteins
â??CON-CONâ?? assignment strategy for highly flexible intrinsically disordered proteins
Abstract
Intrinsically disordered proteins (IDPs) are a class of highly flexible proteins whose characterization by NMR spectroscopy is complicated by severe spectral overlaps. The development of experiments designed to facilitate the sequence-specific assignment procedure is thus very important to improve the tools for the characterization of IDPs and thus to be able to focus on IDPs of increasing size and complexity. Here, we present and describe the...
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10-21-2014 11:31 PM
Longitudinal exchange: an alternative strategy towards quantification of dynamics parameters in ZZ exchange spectroscopy
Longitudinal exchange: an alternative strategy towards quantification of dynamics parameters in ZZ exchange spectroscopy
Abstract Longitudinal exchange experiments facilitate the quantification of the rates of interconversion between the exchanging species, along with their longitudinal relaxation rates, by analyzing the time-dependence of direct correlation and exchange cross peaks. Here we present a simple and robust alternative to this strategy, which is based on the combination of two complementary experiments, one with and one without resolving exchange cross peaks. We show that...
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09-30-2011 08:01 PM
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
J Phys Chem B. 2011 May 2;
Authors: Hwang S, Shao Q, Williams H, Hilty C, Gao YQ
A combined simulation and experimental study was performed to investigate how methanol affects the structure of a model peptide BBA5. BBA5 forms a stable ?-hairpin-?-helix structure in aqueous solutions....
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05-04-2011 04:14 PM
[NMR paper] A strategy for the NMR characterization of type II copper(II) proteins: the case of t
A strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas Syringae.
Related Articles A strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas Syringae.
J Am Chem Soc. 2003 Jun 18;125(24):7200-8
Authors: Arnesano F, Banci L, Bertini I, Felli IC, Luchinat C, Thompsett AR
CopC from Pseudomonas syringae was found to be a protein capable of binding both Cu(I) and Cu(II) at two different...
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11-24-2010 09:01 PM
Strategy for complete NMR assignment of disordered proteins with highly repetitive se
Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution-enhanced 5D experiments
Abstract A strategy for complete backbone and side-chain resonance assignment of disordered proteins with highly repetitive sequence is presented. The protocol is based on three resolution-enhanced NMR experiments: 5D HN(CA)CONH provides sequential connectivity, 5D HabCabCONH is utilized to identify amino acid types, and 5D HC(CC-TOCSY)CONH is used to assign the side-chain resonances. The improved resolution was achieved by a combination of high...
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10-06-2010 02:16 AM
Strategy for complete NMR assignment of disordered proteins with highly repetitive se
Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution-enhanced 5D experiments.
Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution-enhanced 5D experiments.
J Biomol NMR. 2010 Oct 2;
Authors: MotáÄ?ková V, NováÄ?ek J, Zawadzka-Kazimierczuk A, Kazimierczuk K, ZĂ*dek L, Sanderová H, KrásnĂ˝ L, KoĹşmiĹ?ski W, SklenáĹ? V
A strategy for complete backbone and side-chain resonance assignment of disordered proteins with highly...
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10-05-2010 12:11 PM
[NMR paper] NMR strategy for determining Xaa-Pro peptide bond configurations in proteins: mutants
NMR strategy for determining Xaa-Pro peptide bond configurations in proteins: mutants of staphylococcal nuclease with altered configuration at proline-117.
Related Articles NMR strategy for determining Xaa-Pro peptide bond configurations in proteins: mutants of staphylococcal nuclease with altered configuration at proline-117.
Biochemistry. 1993 Nov 9;32(44):11810-8
Authors: Hinck AP, Eberhardt ES, Markley JL
A general approach has been developed for configurational analysis (cis or trans) of Xaa-Pro peptide bonds in proteins. This approach,...
Charges in Hydrophobic Environments: A Strategy forIdentifying Alternative States in Proteins
Linear Mode
