Related ArticlesSolution structure of regioselectively addressable functionalized templates: an NMR and restrained molecular dynamics investigation.
Biopolymers. 1996 Sep;39(3):297-308
Authors: Dumy P, Eggleston IM, Esposito G, Nicula S, Mutter M
Three cyclic peptides that are Regioselectively Addressable Functionalized Templates (RAFT) for use in protein de novo design have been investigated using a combination of nmr, restrained molecular dynamics, and CD spectroscopy. These peptides contain up to four selectively addressable sites (orthogonally protected lysine side chains) or have selectively addressable faces. The results show a common stable conformation for templates of this kind based on two type II beta-turns and an associated beta-sheet structure. A preferential orientation for the side chains is also demonstrated. The significance of these findings is discussed in the context of applications of RAFT that rely on their conformational rigidity and ability to present functionalities in a defined spatial arrangement.
Deuterium Magic Angle Spinning NMR Used to Study the Dynamics of Peptides Adsorbed onto Polystyrene and Functionalized Polystyrene Surfaces.
Deuterium Magic Angle Spinning NMR Used to Study the Dynamics of Peptides Adsorbed onto Polystyrene and Functionalized Polystyrene Surfaces.
Deuterium Magic Angle Spinning NMR Used to Study the Dynamics of Peptides Adsorbed onto Polystyrene and Functionalized Polystyrene Surfaces.
J Phys Chem B. 2011 Jun 8;
Authors: Breen NF, Li K, Olsen GL, Drobny GP
LK?14 is a 14 amino acid peptide which displays a periodic alternation of leucine and lysine amino acids. This "hydrophobic periodicity" has been found to result in an ?-helical secondary structure...
Fast Characterization of Functionalized Silica Materials by Silicon-29 Surface-Enhanced NMR Spectroscopy Using Dynamic Nuclear Polarization
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Moreno Lelli, David Gajan, Anne Lesage, Marc A. Caporini, Veronika Vitzthum, Pascal Mie?ville, Florent He?roguel, Fernando Rasco?n, Arthur Roussey, Chloe? Thieuleux, Malika Boualleg, Laurent Veyre, Geoffrey Bodenhausen, Christophe Cope?ret and Lyndon Emsley
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Journal of the American Chemical Society...
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[NMR paper] NMR structure note--solution structure of a bacterial BolA-like protein XC975 from a
NMR structure note--solution structure of a bacterial BolA-like protein XC975 from a plant pathogen Xanthomonas campestris pv. campestris.
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J Biomol NMR. 2005 Feb;31(2):167-72
Authors: Chin KH, Lin FY, Hu YC, Sze KH, Lyu PC, Chou SH
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[NMR paper] Studies on solution NMR structure of brazzein : Secondary structure and molecular sca
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Sci China C Life Sci. 1999 Aug;42(4):409-19
Authors: Gao G, Dai J, Ding M, Hellekant G, Wang J, Wang D
Brazzein is a sweet-tasting protein isolated from the fruit of West African plantPentadiplandra brazzeana Baillon. It is the smallest and the most water-soluble sweet protein discovered so far and is highly thermostable. The proton NMR study of...
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NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
J Biomol NMR. 2010 Aug;47(4):283-8
Authors: Chen J, Li Q, Liu CC, Zhou B, Bu G, Wang J
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NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6
Content Type Journal Article
DOI 10.1007/s10858-010-9426-8
Authors
Jianglei Chen, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA
Qianqian Li, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA
Chia-Chen Liu, Washington University Departments of Pediatrics, and Cell Biology and Physiology, School of Medicine St. Louis MO 63110 USA