Related ArticlesDynamical 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 correlation times is used to analyze the nanosecond time-scale dynamics of the partially unfolded domain 2 of annexin I from its (15)N NMR relaxation parameters measured at three magnetic field strengths. The use of a distribution of correlation times enables the characterization of the dynamical features of the NH bonds of the protein in terms of heterogeneity of dynamical states in the nanosecond range. The variation along the sequence of the two dynamical parameters introduced, namely the center and the width of the distribution, points out the different types of residual secondary structures present in the D2 domain. Moreover, it allows a physically sensible interpretation of the dynamical behavior of the different residual helices and of the non-native structures. Also, a striking correspondence is found between the parameters obtained using an extended Lipari and Szabo model and the parameters obtained using the distribution of correlation times. This result led us to propose a specific interpretation of the model-free order parameter for internal motions in the nanosecond range in the case of unfolded states.
[NMR paper] Generation of native-like protein structures from limited NMR data, modern force fiel
Generation of native-like protein structures from limited NMR data, modern force fields and advanced conformational sampling.
Related Articles Generation of native-like protein structures from limited NMR data, modern force fields and advanced conformational sampling.
J Biomol NMR. 2005 Jan;31(1):59-64
Authors: Chen J, Won HS, Im W, Dyson HJ, Brooks CL
Determining an accurate initial native-like protein fold is one of the most important and time-consuming steps of de novo NMR structure determination. Here we demonstrate that high-quality...
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[NMR paper] NMR characterization of native liquid spider dragline silk from Nephila edulis.
NMR characterization of native liquid spider dragline silk from Nephila edulis.
Related Articles NMR characterization of native liquid spider dragline silk from Nephila edulis.
Biomacromolecules. 2004 May-Jun;5(3):834-9
Authors: Hronska M, van Beek JD, Williamson PT, Vollrath F, Meier BH
Solid spider dragline silk is well-known for its mechanical properties. Nonetheless a detailed picture of the spinning process is lacking. Here we report NMR studies on the liquid silk within the wide sac of the major ampullate (m.a.) gland from the spider...
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[NMR paper] Elucidation of the structures of residual and dissolved pine kraft lignins using an H
Elucidation of the structures of residual and dissolved pine kraft lignins using an HMQC NMR technique.
Related Articles Elucidation of the structures of residual and dissolved pine kraft lignins using an HMQC NMR technique.
J Agric Food Chem. 2003 Oct 8;51(21):6116-27
Authors: Balakshin MY, Capanema EA, Chen CL, Gracz HS
Comparative studies on the structures of residual and dissolved lignins isolated from pine kraft pulp and pulping liquor have been undertaken using the (1)H-(13)C HMQC NMR technique, GPC, and sugar analysis to elucidate the...
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[NMR paper] The importance of being ordered: improving NMR structures using residual dipolar coup
The importance of being ordered: improving NMR structures using residual dipolar couplings.
Related Articles The importance of being ordered: improving NMR structures using residual dipolar couplings.
C R Biol. 2002 Sep;325(9):957-66
Authors: Gronenborn AM
Residual dipolar couplings arise from small degrees of alignment of molecules in a magnetic field. Most biomolecules lack sufficient intrinsic magnetic susceptibility anisotropies for practical purposes; however, alignment can be achieved using dilute aqueous phospholipid mixtures, colloidal...
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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 characterization of the molten globule and native states of ovalbumin: a 1
Structural characterization of the molten globule and native states of ovalbumin: a 1H NMR study.
Related Articles Structural characterization of the molten globule and native states of ovalbumin: a 1H NMR study.
J Pept Res. 1997 Dec;50(6):465-74
Authors: Sogami M, Era S, Koseki T, Nagai N
Molecular characteristics of ovalbumin (OVA) in the acidic (pD 3.08, the E-form) and neutral regions were studied by measuring effective radii, 1H NMR spectra, spin-echo 1H NMR spectra and cross-relaxation times (TIS) from irradiated to observed protein...
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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...
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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...
Dynamical characterization of residual and non-native structures in a partially folde
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