Related ArticlesStructural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy.
Protein Sci. 1995 Dec;4(12):2605-15
Authors: Frank MK, Clore GM, Gronenborn AM
The structure and dynamics of the urea-denatured B1 immunoglobulin binding domain of streptococcal protein G (GB1) has been investigated by multidimensional heteronuclear NMR spectroscopy. Complete 1H, 15N, and 13C assignments are obtained by means of sequential through-bond correlations. The nuclear Overhauser enhancement, chemical shift, and 3JHN alpha coupling constant data provide no evidence for the existence of any significant population of residual native or nonnative ordered structure. 15N relaxation measurements at 500 and 600 MHz, however, provide evidence for conformationally restricted motions in three regions of the polypeptide that correspond to the second beta-hairpin, the N-terminus of the alpha-helix, and the middle of the alpha-helix in the native protein. The time scale of these motions is longer than the apparent overall correlation time (approximately 3 ns) and could range from about 6 ns in the case of one model to between 4 microseconds and 2 ms in another; it is not possible to distinguish between these two cases with certainty because the dynamics are highly complex and hence the analysis of the time scale of this slower motion is highly model dependent. It is suggested that these three regions may correspond to nucleation sites for the folding of the GB1 domain. With the exception of the N- and C-termini, where end effects predominate, the amplitude of the subnanosecond motions, on the other hand, are fairly uniform and model independent, with an overall order parameter S2 ranging from 0.4 to 0.5.
[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] A comparison of the pH, urea, and temperature-denatured states of barnase by heteronu
A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.
J Mol Biol. 1995 Nov 24;254(2):305-21
Authors: Arcus VL, Vuilleumier S, Freund SM, Bycroft M, Fersht AR
The denatured states of...
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[NMR paper] Structural and dynamic characterization of the phosphotyrosine binding region of a Sr
Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain--phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches.
Related Articles Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain--phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches.
Biochemistry. 1995 Sep 12;34(36):11353-62
Authors: Pascal SM, Yamazaki T, Singer AU, Kay LE, Forman-Kay JD
Arginine side chains are often...
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[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 determination of residual structure in a urea-denatured protein, the 434-represso
NMR determination of residual structure in a urea-denatured protein, the 434-repressor.
Related Articles NMR determination of residual structure in a urea-denatured protein, the 434-repressor.
Science. 1992 Sep 11;257(5076):1559-63
Authors: Neri D, Billeter M, Wider G, Wüthrich K
A nuclear magnetic resonance (NMR) structure determination is reported for the polypeptide chain of a globular protein in strongly denaturing solution. Nuclear Overhauser effect (NOE) measurements with a 7 molar urea solution of the amino-terminal 63-residue domain...
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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 and dynamic characterization of the urea denatured state of the immunoglob
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