[NMR paper] Combined use of optical spectroscopy and computational methods to study the binding and the photoinduced conformational modification of proteins when NMR and x-ray structural determinations are not an option.
Combined use of optical spectroscopy and computational methods to study the binding and the photoinduced conformational modification of proteins when NMR and x-ray structural determinations are not an option.
Related ArticlesCombined use of optical spectroscopy and computational methods to study the binding and the photoinduced conformational modification of proteins when NMR and x-ray structural determinations are not an option.
Adv Protein Chem Struct Biol. 2013;93:95-152
Authors: Brancaleon L
Abstract
The functions of proteins depend on their interactions with various ligands and these interactions are controlled by the structure of the polypeptides. If one can manipulate the structure of proteins, their functions can in principle be modulated. The issue of protein structure-function relationship is not only a central problem in biophysics, but is becoming clear that the ability to "artificially" modify the structure of proteins could be relevant in fields beyond the biomedical area to provide, for instance, light responses in proteins which would not possess such properties in their native state. This chapter presents an overview of the combination of optical electronic and vibrational spectroscopy with various computational methods to investigate the binding between photoactive ligands and proteins.
[NMR paper] Impact of oxidized phospholipids on the structural and dynamic organization of phospholipid membranes: a combined DSC and solid state NMR study.
Impact of oxidized phospholipids on the structural and dynamic organization of phospholipid membranes: a combined DSC and solid state NMR study.
Impact of oxidized phospholipids on the structural and dynamic organization of phospholipid membranes: a combined DSC and solid state NMR study.
Faraday Discuss. 2013;161:499-513; discussion 563-89
Authors: Wallgren M, Beranova L, Pham QD, Linh K, Lidman M, Procek J, Cyprych K, Kinnunen PK, Hof M, Gröbner G
Abstract
Membranes undergo severe changes under oxidative stress conditions due to the...
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06-29-2013 11:49 AM
[NMR paper] Structural characterization of a peptoid with lysine-like side chains and biological activity using NMR and computational methods.
Structural characterization of a peptoid with lysine-like side chains and biological activity using NMR and computational methods.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Structural characterization of a peptoid with lysine-like side chains and biological activity using NMR and computational methods.
Org Biomol Chem. 2013 Jan 28;11(4):640-7
Authors: Sternberg U, Birtalan E, Jakovkin I, Luy B, Schepers U, Bräse S, Muhle-Goll C
Abstract
...
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06-05-2013 06:53 PM
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
J Phys Chem B. 2011 May 2;
Authors: Hwang S, Shao Q, Williams H, Hilty C, Gao YQ
A combined simulation and experimental study was performed to investigate how methanol affects the structure of a model peptide BBA5. BBA5 forms a stable ?-hairpin-?-helix structure in aqueous solutions....
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05-04-2011 04:14 PM
Alkali Metals in Ethylenediamine: A Computational Study of the Optical Absorption Spectra and NMR Parameters of [M(en)3?+·M?-] Ion Pairs
Alkali Metals in Ethylenediamine: A Computational Study of the Optical Absorption Spectra and NMR Parameters of Ion Pairs
Eva Zurek
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1085244/aop/images/medium/ja-2010-085244_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1085244
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/iq3xbI47u0Y
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03-03-2011 02:06 AM
Structural and Binding Study of Modified siRNAs with the Argonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Argonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Argonaute 2 PAZ Domain by NMR Spectroscopy.
Chemistry. 2011 Feb 1;17(5):1519-1528
Authors: Maiti M, Nauwelaerts K, Lescrinier E, Herdewijn P
By using high-resolution NMR spectroscopy, the structures of a natural short interfering RNA (siRNA) and of several altritol nucleic acid (ANA)-modified siRNAs were determined. The interaction of modified siRNAs with the PAZ domain of the Argonaute...
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01-27-2011 02:52 PM
Structural and Binding Study of Modified siRNAs with the Agonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Agonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Agonaute 2 PAZ Domain by NMR Spectroscopy.
Chemistry. 2011 Jan 5;
Authors: Maiti M, Nauwelaerts K, Lescrinier E, Herdewijn P
By using high-resolution NMR spectroscopy, the structures of a natural short interfering RNA (siRNA) and of several altritol nucleic acid (ANA)-modified siRNAs were determined. The interaction of modified siRNAs with the PAZ domain of the Argonaute 2 protein of...
[NMR paper] Structural genomics and the metabolome: combining computational and NMR methods to id
Structural genomics and the metabolome: combining computational and NMR methods to identify target ligands.
Related Articles Structural genomics and the metabolome: combining computational and NMR methods to identify target ligands.
Curr Opin Drug Discov Devel. 2004 Jan;7(1):62-8
Authors: Parsons L, Orban J
One of the goals of structural genomics is to use three-dimensional structures to gain insights into the function of poorly understood or hypothetical proteins. Approximate functions are often apparent from the protein fold, but more...
Combined use of optical spectroscopy and computational methods to study the binding and the photoinduced conformational modification of proteins when NMR and x-ray structural determinations are not an option.
Linear Mode
