Related ArticlesProbing protein structure by solvent perturbation of NMR spectra. Photochemically induced dynamic nuclear polarization and paramagnetic perturbation techniques applied to the study of the molten globule state of alpha-lactalbumin.
Eur J Biochem. 1995 Jan 15;227(1-2):87-96
Authors: Improta S, Molinari H, Pastore A, Consonni R, Zetta L
We have characterized the high-temperature molten globule state of bovine alpha-lactalbumin by a combined use of photochemically induced dynamic nuclear polarization and nitroxide surface perturbation. Both techniques are extremely well suited to follow the progressive increase of exposed surfaces in the native state and the appearance of partially or completely unfolded species. Our results suggest that the molten globule state obtained at high temperature and pH 7, and the state obtained at pH 2 are not only thermodynamically but also structurally very similar.
Singular spectrum analysis for an automated solvent artifact removal and baseline correction of 1D NMR spectra.
Singular spectrum analysis for an automated solvent artifact removal and baseline correction of 1D NMR spectra.
Singular spectrum analysis for an automated solvent artifact removal and baseline correction of 1D NMR spectra.
J Magn Reson. 2011 Mar 6;
Authors: De Sanctis S, Malloni WM, Kremer W, Tomé AM, Lang EW, Neidig KP, Kalbitzer HR
NMR spectroscopy in biology and medicine is generally performed in aqueous solutions, thus in (1)H NMR spectroscopy, the dominant signal often stems from the partly suppressed solvent and can be many orders of...
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[NMR paper] Probing membrane protein orientation and structure using fast magic-angle-spinning so
Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR.
Related Articles Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR.
J Biomol NMR. 2004 Nov;30(3):253-65
Authors: Andronesi OC, Pfeifer JR, Al-Momani L, Ozdirekcan S, Rijkers DT, Angerstein B, Luca S, Koert U, Killian JA, Baldus M
One and two-dimensional solid-state NMR experiments are discussed that permit probing local structure and overall molecular conformation of membrane-embedded polypeptides...
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[NMR paper] Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
Related Articles Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
J Biol Chem. 2004 Feb 13;279(7):5699-707
Authors: Olofsson A, Ippel JH, Wijmenga SS, Lundgren E, Ohman A
The human plasma protein transthyretin (TTR) may form fibrillar protein deposits that are associated with both inherited and idiopathic amyloidosis. The present study utilizes solution nuclear magnetic resonance spectroscopy, in combination with...
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[NMR paper] Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
Related Articles Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8648-53
Authors: Ippel JH, Olofsson A, Schleucher J, Lundgren E, Wijmenga SS
Amyloid is the result of an anomalous protein and peptide aggregation, leading to the formation of insoluble fibril deposits. At present, 18 human diseases have been associated with amyloid deposits-e.g., Alzheimer's disease and Prion-transmissible...
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[NMR paper] Probing protein structure by solvent perturbation of NMR spectra: the surface accessi
Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor.
Biophys J. 1997 Jul;73(1):382-96
Authors: Molinari H,...
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[NMR paper] Probing protein structure by solvent perturbation of NMR spectra: the surface accessi
Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor.
Biophys J. 1997 Jul;73(1):382-96
Authors: Molinari H,...
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08-22-2010 03:03 PM
[NMR paper] Probing protein structure by solvent perturbation of NMR spectra. A comparison with p
Probing protein structure by solvent perturbation of NMR spectra. A comparison with photochemically induced dynamic nuclear polarization techniques applied to native alpha-lactalbumin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Probing protein structure by solvent perturbation of NMR spectra. A comparison with photochemically induced dynamic nuclear polarization techniques applied to native alpha-lactalbumin.
Eur J Biochem. 1995 Jan 15;227(1-2):78-86...
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[NMR paper] Probing protein structure by solvent perturbation of NMR spectra. II. Determination o
Probing protein structure by solvent perturbation of NMR spectra. II. Determination of surface and buried residues in homologous proteins.
Related Articles Probing protein structure by solvent perturbation of NMR spectra. II. Determination of surface and buried residues in homologous proteins.
Biopolymers. 1993 May;33(5):839-46
Authors: Esposito G, Lesk AM, Molinari H, Motta A, Niccolai N, Pastore A
The experimental assignment of most residues in a protein to the surface or interior is in principle possible without prior solution of a complete...