[NMR paper] Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Related Articles Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Biomol NMR Assign. 2013 Jul 3;
Authors: Hsieh SJ, Mallam AL, Jackson SE, Hsu ST
Abstract
YbeA is a 3-methylpseudoridine methyltransferase from Escherichia coli that forms a stable homodimer in solution. It is one of the deeply trefoil 31 knotted proteins, of which the knot encompasses the C-terminal helix that threads through a long loop. Recent...
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07-05-2013 08:03 AM
[NMR paper] NMR and SAXS characterization of the denatured state of the chemotactic protein CheY:
NMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiation.
Related Articles NMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiation.
Protein Sci. 2001 Jun;10(6):1100-12
Authors: Garcia P, Serrano L, Durand D, Rico M, Bruix M
The denatured state of a double mutant of the chemotactic protein CheY (F14N/V83T) has been analyzed in the presence of 5 M urea, using small angle X-ray scattering (SAXS) and...
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11-19-2010 08:32 PM
[NMR paper] NMR characterization of residual structure in the denatured state of protein L.
NMR characterization of residual structure in the denatured state of protein L.
Related Articles NMR characterization of residual structure in the denatured state of protein L.
J Mol Biol. 2000 Jun 23;299(5):1341-51
Authors: Yi Q, Scalley-Kim ML, Alm EJ, Baker D
Triple-resonance NMR experiments were used to assign the (13)C(alpha), (13)C(beta), (15)N and NH resonances for all the residues in the denatured state of a destabilized protein L variant in 2 M guanidine. The chemical shifts of most resonances were very close to their random coil...
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11-18-2010 09:15 PM
[NMR paper] Microscopic stability of cold shock protein A examined by NMR native state hydrogen e
Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide.
Related Articles Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide.
Protein Sci. 2000 Feb;9(2):290-301
Authors: Jaravine VA, Rathgeb-Szabo K, Alexandrescu AT
Native state hydrogen exchange of cold shock protein A (CspA) has been characterized as a function of the denaturant urea and of the stabilizing agent...
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11-18-2010 09:15 PM
[NMR paper] NMR assignments for acid-denatured cold shock protein A.
NMR assignments for acid-denatured cold shock protein A.
Related Articles NMR assignments for acid-denatured cold shock protein A.
J Biomol NMR. 1998 May;11(4):461-2
Authors: Alexandrescu AT, Rathgeb-Szabo K
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11-17-2010 11:06 PM
[NMR paper] Structural and dynamic characterization of the urea denatured state of the immunoglob
Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal...
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08-22-2010 03:50 AM
[MWClarkson blog] How native-like is a cold-denatured structure?
How native-like is a cold-denatured structure?
http://www.researchblogging.org/public/citation_icons/rb2_large_gray.pngA protein has several different levels of structure. The primary structure is the arrangements of atoms and bonds, and it is formed in the ribosome by the assembly of amino acids as directed by an RNA template. The secondary structure is the local topology, the helices and strands, and this forms mostly because of the release of energy through the formation of hydrogen bonds. The tertiary structure is the actual fold of the protein, the way helices, strands, and loops are...
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08-22-2010 01:58 AM
[NMR paper] Characterization of a partially denatured state of a protein by two-dimensional NMR:
Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin.
Related Articles Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin.
Biochemistry. 1991 Mar 26;30(12):3120-8
Authors: Harding MM, Williams DH, Woolfson DN
A stable, partially structured state of ubiquitin, the A-state, is formed at pH 2.0 in 60% methanol/40% water at 298 K. Detailed characterization of the structure...
an paper about the cold denatured state of protein
Linear Mode
