A Gradient of Sitewise Diversity Promotes EvolutionaryFitness for Binder Discovery in a Three-Helix Bundle Protein Scaffold
A Gradient of Sitewise Diversity Promotes EvolutionaryFitness for Binder Discovery in a Three-Helix Bundle Protein Scaffold
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Biochemistry
DOI: 10.1021/acs.biochem.6b01142
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Deletion of the N- or C-Terminal Helix of ApolipophorinIII To Create a Four-Helix Bundle Protein
Deletion of the N- or C-Terminal Helix of ApolipophorinIII To Create a Four-Helix Bundle Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00381/20160623/images/medium/bi-2016-00381k_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00381
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06-24-2016 12:27 AM
[NMR paper] Probing the Residual Structure of the Low Populated Denatured State of ADA2h under Folding Conditions by Relaxation Dispersion NMR Spectroscopy.
Probing the Residual Structure of the Low Populated Denatured State of ADA2h under Folding Conditions by Relaxation Dispersion NMR Spectroscopy.
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Biochemistry. 2015 Jun 26;
Authors: Pustovalova Y, Kukic P, Vendruscolo M, Korzhnev DM
Abstract
The structural characterization of low-populated states of proteins with accuracy comparable to that achievable for native states is...
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06-27-2015 01:13 PM
[NMR paper] Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
Related Articles Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
J Mol Biol. 2013 Nov 15;
Authors: Sackett K, Nethercott MJ, Zheng Z, Weliky DP
Abstract
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although...
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11-20-2013 12:52 PM
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Publication date: Available online 16 November 2013
Source:Journal of Molecular Biology</br>
Author(s): Kelly Sackett , Matthew J. Nethercott , Zhaoxiong Zheng , David P. Weliky</br>
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although the ~20-residue N-terminal fusion peptide (FP) region is critical for fusion, the structure of this region is not...
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11-16-2013 03:14 PM
[NMR paper] Redesign of a four-helix bundle protein by phage display coupled with proteolysis and
Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography.
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J Mol Biol. 2002 Oct 18;323(2):253-62
Authors: Chu R, Takei J, Knowlton JR, Andrykovitch M, Pei W, Kajava AV, Steinbach PJ, Ji X, Bai Y
To test whether it is practical to use phage display coupled with proteolysis for protein design, we...
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11-24-2010 08:58 PM
[NMR paper] Dynamics of a de novo designed three-helix bundle protein studied by 15N, 13C, and 2H
Dynamics of a de novo designed three-helix bundle protein studied by 15N, 13C, and 2H NMR relaxation methods.
Related Articles Dynamics of a de novo designed three-helix bundle protein studied by 15N, 13C, and 2H NMR relaxation methods.
Biochemistry. 2001 Aug 14;40(32):9560-9
Authors: Walsh ST, Lee AL, DeGrado WF, Wand AJ
Understanding how the amino acid sequence of a polypeptide chain specifies a unique, functional three-dimensional structure remains an important goal, especially in the context of the emerging discipline of de novo protein...
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11-19-2010 08:44 PM
[NMR paper] Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on huma
Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on human interleukin-4.
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Biochemistry. 1992 Nov 3;31(43):10431-7
Authors: Redfield C, Boyd J, Smith LJ, Smith RA, Dobson CM
15N NOE, T1, and T2 measurements have been carried out on uniformly 15N-labeled human interleukin-4. Analysis of the results in terms of order parameters (S2) shows that although the helical core of this four-helix-bundle protein...
Probing Denatured State Conformational Bias in a Three-Helix Bundle, UBA(2), Using a Cytochrome c Fusion Protein
Linear Mode
