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Proteins structure, nuclear magnetic resonance

INSIGHTS INTO THE STRUCTURE AND DYNAMICS OF UNFOLDED PROTEINS FROM NUCLEAR MAGNETIC RESONANCE... [Pg.334]

R. B. Altman and O. Jardetzky, in Methods in Enzymology, Vol. 177, N. J. Oppenheimer and T. L. James, Eds., Academic Press, San Diego, Calif., 1989, pp. 218-246. Heuristic Refinement Method for Determination of Solution Structure of Proteins from Nuclear Magnetic Resonance Data. [Pg.168]

R239 J. D. Baleja, Structure Determination of Membrane-Associated Proteins from Nuclear Magnetic Resonance Data , Anal. Biochem., 2001, 288, 1... [Pg.19]

R542 N. J. Skelton and W. J. Chazin, Solution Structure Determination of Proteins by Nuclear Magnetic Resonance Spectroscopy , Drugs Pharm. Sci., 2000,101, 683... [Pg.37]

R616 M. Zhang and P. Yang, Determination of the Secondary Structure of Proteins by Nuclear Magnetic Resonance , Huaxue Tongbao, 2000, 12, 26... [Pg.42]

R 313 D. Shortle, The Expended Denatured State An Ensemble of Conformations Trapped in a Locally Encoded Topological Space , p. 1 R 314 H.J. Dyson and P.E. Wright, Insights into the Structure and Dynamics of Unfolded Proteins from Nuclear Magnetic Resonance , p. 311... [Pg.28]

R 785 F. del Rio Portilla, Structural Analysis of Proteins by Nuclear Magnetic Resonance and Mass Spectrometry , Educacion Quimica, 2003,14,9 R 786 G. G. Gallego, Revolutionary Methods for the Analysis of Macromolecules , Anales de la Real Academia Nacional de Farmada, 2003,69,71 R 787 J. M. Natta and M. Gari, Contribution of Isotopic Methods ( H-NMR and C-MS) to the Alcoholic Beverage Industry for Confirming Brandy Authenticity , Alimentacion, Equipos y Tecnologia, 2003,183,47... [Pg.56]

Panjwrmi, N., Hodgson, D.J., Sauve, S., Aubin, Y. (2010) Assessment of the effects of pH, formulation and deformulation on the conformation of interferon alpha-2 by NMR. J Pharm Sci, 99 (8), 3334-3342. Amezcua, C.A., Szabo, C.M. (2013) Assessment of higher order structure comparability in therapeutic proteins using nuclear magnetic resonance spectroscopy. J Pharm Sci, 102 (6), 1724—1733. [Pg.339]

R613 F. Hagn and H. Kessler, Spider Silk Proteins. Structure and Function of Spider Silk Proteins by Nuclear Magnetic Resonance Spectroscopy , GIT Lahor-Fachzeitschrift, 2011, 55, 838. [Pg.61]

S. J. Opella, Structure Determination of Membrane Proteins by Nuclear Magnetic Resonance Spectroscopy, Annu. Rev. Anal Chem., 2013, 6, 305. [Pg.29]

Bioenergetics Hydrogen Bond Macro-molecules, Structure Membrane Structure Nuclear Magnetic Resonance (NMR) Protein Folding Protein Synthesis X-Ray Analysis... [Pg.178]

TF Flavel. An evaluation of computational strategies for use m the determination of protein structure from distance constraints obtained by nuclear magnetic resonance. Prog Biophys Mol Biol 56 43, 1991. [Pg.90]

GM Clore, MA Robien, AM Gronenborn. Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy. J Mol Biol 231 82-102, 1993. [Pg.310]

Wiithrich, K. Protein structure determination in solution by nuclear magnetic resonance spectroscopy. Science 243 45-50, 1989. [Pg.392]

The use of computer simulations to study internal motions and thermodynamic properties is receiving increased attention. One important use of the method is to provide a more fundamental understanding of the molecular information contained in various kinds of experiments on these complex systems. In the first part of this paper we review recent work in our laboratory concerned with the use of computer simulations for the interpretation of experimental probes of molecular structure and dynamics of proteins and nucleic acids. The interplay between computer simulations and three experimental techniques is emphasized (1) nuclear magnetic resonance relaxation spectroscopy, (2) refinement of macro-molecular x-ray structures, and (3) vibrational spectroscopy. The treatment of solvent effects in biopolymer simulations is a difficult problem. It is not possible to study systematically the effect of solvent conditions, e.g. added salt concentration, on biopolymer properties by means of simulations alone. In the last part of the paper we review a more analytical approach we have developed to study polyelectrolyte properties of solvated biopolymers. The results are compared with computer simulations. [Pg.82]

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See also in sourсe #XX -- [ Pg.38 ]



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