Related ArticlesStructural characterization of monellin in the alcohol-denatured state by NMR: evidence for beta-sheet to alpha-helix conversion.
Biochemistry. 1993 Feb 16;32(6):1573-82
Authors: Fan P, Bracken C, Baum J
Two-dimensional 1H NMR spectroscopy and hydrogen exchange methods have been used to characterize the alcohol-denatured state of monellin. Monellin is a sweet tasting protein composed of two chains. In the native state, the A-chain consists entirely of beta-structure, and the B-chain contains both alpha- and beta-structure. Upon addition of either 50% ethanol or 50% trifluoroethanol (TFE), the native structure of monellin is disrupted resulting in an alcohol-denatured state with properties different from those of the random coil state. In the alcohol-denatured state, the far-UV circular dichroism (CD) spectrum displays a higher helical content relative to the native state and the intensity of the near-UV CD signal is completely lost. One-dimensional NMR studies show that there are approximately 14 amide protons protected from exchange with solvent in the alcohol-denatured state and that large portions of the protein exchange at a rate that is comparable to the exchange rate of the protein in urea. Utilizing hydrogen exchange trapping techniques, the slowly exchanging residues are identified at pH 2.0 in 50% ethanol and 50% TFE (A10-A15, A18, A19, A21, A24, and A39) and are found to be clustered on one region of the A-chain. Preliminary 2D NMR assignments show that in the alcohol-denatured state the A-chain of monellin undergoes structural reorganization, with one strand of the native state beta-sheet on the A-chain (residues A17-A30) becoming an alpha-helix in the alcohol-denatured state. The secondary structure of the A-chain in the alcohol-denatured state is different from the native state structure, although the slowly exchanging residues are similar.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State Magic-Angle-Spinning NMR
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State Magic-Angle-Spinning NMR
Riqiang Fu, Xingsheng Wang, Conggang Li, Adriana N. Santiago-Miranda, Gary J. Pielak and Fang Tian
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja204062v/aop/images/medium/ja-2011-04062v_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja204062v
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/BuOPwKpaHdw
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In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
J Am Chem Soc. 2011 Jul 21;
Authors: Fu R, Wang X, Li C, Santiago-Miranda AN, Pielak GJ, Tian F
The feasibility of using solid state MAS NMR for in situ structural characterization of the LR11 (sorLA) transmembrane domain in native Escherichia coli (E. coli) membranes is presented. LR11 interacts with...
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Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
J Mol Biol. 2011 Jul 13;
Authors: Schneider R, Schumacher MC, Mueller H, Nand D, Klaukien V, Heise H, Riedel D, Wolf G, Behrmann E, Raunser S, Seidel R, Engelhard M, Baldus M
Protein aggregation via polyglutamine stretches occurs in a number of severe neurodegenerative diseases such as Huntington's disease. We have investigated fibrillar aggregates of polyglutamine peptides...
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[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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[NMR paper] NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobi
NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding.
Related Articles NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding.
Biochemistry. 2001 Mar 27;40(12):3561-71
Authors: Yao J, Chung J, Eliezer D, Wright PE, Dyson HJ
Apomyoglobin forms a denatured state under low-salt conditions at pH 2.3. The conformational propensities and polypeptide backbone dynamics...
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[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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[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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[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...
Structural characterization of monellin in the alcohol-denatured state by NMR: eviden
Linear Mode
