Related ArticlesCharacterization 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 of this state has been carried out by 2D NMR spectroscopy. Assignment of slowly exchanging amide resonances protected from the solvent in the native and A-state shows that gross structural reorganization of the protein has not occurred and that the A-state contains a subset of the interactions present in the native state (N-state). Vicinal coupling constants and NOESY data show the presence of the first two strands of the five-strand beta-sheet that is present in the native protein and part of the third beta-strand. The hydrophobic face of the beta-sheet in the A-state is covered by a partially structured alpha-helix, tentatively assigned to residues 24-34, that is considerably more flexible than the alpha-helix in the N-state. There is evidence for some fixed side-chain--side-chain interactions between these two units of structure. The turn-rich area of the protein, which contains seven reverse turns and a short piece of 3(10) helix, does not appear to be structured in the A-state and is approaching random coil.
[NMR paper] Dynamical characterization of residual and non-native structures in a partially folde
Dynamical characterization of residual and non-native structures in a partially folded protein by (15)N NMR relaxation using a model based on a distribution of correlation times.
Related Articles Dynamical characterization of residual and non-native structures in a partially folded protein by (15)N NMR relaxation using a model based on a distribution of correlation times.
Protein Sci. 2002 Apr;11(4):957-64
Authors: Ochsenbein F, Neumann JM, Guittet E, van Heijenoort C
A spectral density model based on a truncated lorentzian distribution of...
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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 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] Ribosomal protein S17: characterization of the three-dimensional structure by 1H and
Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.
Related Articles Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.
Biochemistry. 1993 Nov 30;32(47):12812-20
Authors: Golden BL, Hoffman DW, Ramakrishnan V, White SW
The structure of ribosomal protein S17 from Bacillus stearothermophilus was investigated by two-dimensional homonuclear and heteronuclear magnetic resonance spectroscopy. The 1H and 15N chemical shift assignments are largely complete, and a...
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[NMR paper] Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: th
Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: the A-state of human ubiquitin.
Related Articles Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: the A-state of human ubiquitin.
J Biomol NMR. 1993 May;3(3):285-96
Authors: Stockman BJ, Euvrard A, Scahill TA
Human ubiquitin is a 76-residue protein that serves as a protein degradation signal when conjugated to another protein. Ubiquitin has been shown to exist in at least three states: native (N-state), unfolded (U-state), and,...
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08-21-2010 11:53 PM
[NMR paper] Structural characterization of monellin in the alcohol-denatured state by NMR: eviden
Structural characterization of monellin in the alcohol-denatured state by NMR: evidence for beta-sheet to alpha-helix conversion.
Related Articles Structural 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....
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[NMR paper] NMR characterization of partially folded and unfolded conformational ensembles of pro
NMR characterization of partially folded and unfolded conformational ensembles of proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles NMR characterization of partially folded and unfolded conformational ensembles of proteins.
Biopolymers. 1999;51(3):191-207
Authors: Barbar E
Studies of unfolded and partially folded proteins provide important insight into the initiation and process of protein folding. This review focuses on the...
Characterization of a partially denatured state of a protein by two-dimensional NMR:
Linear Mode
