[NMR paper] Probing the active conformation of FGLamide allatostatin analogs with N-terminal modifications using NMR spectroscopy and molecular modeling.
Related ArticlesProbing the active conformation of FGLamide allatostatin analogs with N-terminal modifications using NMR spectroscopy and molecular modeling.
Peptides. 2015 Jun;68:214-8
Authors: Xie Y, Zhang L, Wu XQ, Zhang CL, Yang XL, Tobe SS
Abstract
The FGLamide allatostatins (ASTs) can inhibit the production of juvenile hormone in vitro, and they therefore are regarded as possible insect growth regulator candidates for pest control. To understand the structural features of the ASTs that cause the differences in their activity the pentapeptide and four N-terminal modifications of AST analogs (H17, K9, K10 and K23) were selected to investigate their conformations. From NMR spectroscopy and molecular modeling, it is clear that K23 and K9 have a type IV ?-turn and a ? turn in DMSO, respectively. The pentapeptide, H17 and K10 form a flexible conformation. Our study indicates that this flexible conformation could be an important and indispensable structural element for activity, whereas the turn structure may not be especially significant for biological activity.
[NMR paper] Structure-Function Analysis of the Non-Muscle Myosin Light Chain Kinase (nmMLCK) Isoform by NMR Spectroscopy and Molecular Modeling: Influence of MYLK Variants.
Structure-Function Analysis of the Non-Muscle Myosin Light Chain Kinase (nmMLCK) Isoform by NMR Spectroscopy and Molecular Modeling: Influence of MYLK Variants.
Related Articles Structure-Function Analysis of the Non-Muscle Myosin Light Chain Kinase (nmMLCK) Isoform by NMR Spectroscopy and Molecular Modeling: Influence of MYLK Variants.
PLoS One. 2015;10(6):e0130515
Authors: Shen K, Ramirez B, Mapes B, Shen GR, Gokhale V, Brown ME, Santarsiero B, Ishii Y, Dudek SM, Wang T, Garcia JG
Abstract
The MYLK gene encodes the...
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06-26-2015 09:55 PM
[NMR images] Probing composition, sequence, and conformation
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2/12/2013 9:37:38 AM GMT
PROBING COMPOSITION, SEQUENCE, AND CONFORMATION
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12-02-2013 09:36 AM
[NMR paper] Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of Phospholipase D1 revealed by NMR spectroscopy.
Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of Phospholipase D1 revealed by NMR spectroscopy.
Related Articles Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of Phospholipase D1 revealed by NMR spectroscopy.
Biochim Biophys Acta. 2013 Apr 19;
Authors: Farina B, Doti N, Pirone L, Malgieri G, Pedone EM, Ruvo M, Fattorusso R
Abstract
PED/PEA15 is a small protein involved in many protein-protein interactions that modulates the function of a number of key cellular effectors involved in...
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04-24-2013 09:48 PM
Probing Dynamic Conformationsof the High-Molecular-Weight?B-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy
Probing Dynamic Conformationsof the High-Molecular-Weight?B-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy
Andrew J. Baldwin, Patrick Walsh, D. Flemming Hansen, Gillian R. Hilton, Justin L. P. Benesch, Simon Sharpe and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja307874r/aop/images/medium/ja-2012-07874r_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja307874r
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09-08-2012 08:44 AM
Probing the HIV gp120 envelope glycoprotein conformation by NMR.
Probing the HIV gp120 envelope glycoprotein conformation by NMR.
Probing the HIV gp120 envelope glycoprotein conformation by NMR.
J Biol Chem. 2011 Jul 8;286(27):23975-81
Authors: Celigoy J, Ramirez B, Tao L, Rong L, Yan L, Feng YR, Quinnan GV, Broder CC, Caffrey M
Abstract
The HIV envelope glycoprotein gp120 plays a critical role in virus entry, and thus, its structure is of extreme interest for the development of novel therapeutics and vaccines. To date, high resolution structural information about gp120 in complex with gp41 has proven...
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09-09-2011 06:42 PM
Development of Non-Peptide Ligands of Growth Factor Receptor-Bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy (†).
Development of Non-Peptide Ligands of Growth Factor Receptor-Bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy (†).
Development of Non-Peptide Ligands of Growth Factor Receptor-Bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy (†).
J Med Chem. 2011 Jan 27;
Authors: Orcajo-Rinco?n AL, Ortega-Gutie?rrez S, Serrano P, Torrecillas IR, Wu?thrich K, Campillo M, Pardo L, Viso A, Benhamu? B, Lo?pez-Rodri?guez ML
We report a novel series of non-peptide ligands that inhibit the growth...
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01-29-2011 12:35 PM
[NMR paper] Active conformations of glycosaminoglycans. NMR determination of the conformation of
Active conformations of glycosaminoglycans. NMR determination of the conformation of heparin sequences complexed with antithrombin and fibroblast growth factors in solution.
Related Articles Active conformations of glycosaminoglycans. NMR determination of the conformation of heparin sequences complexed with antithrombin and fibroblast growth factors in solution.
Semin Thromb Hemost. 2002 Aug;28(4):325-34
Authors: Hricovíni M, Guerrini M, Bisio A, Torri G, Naggi A, Casu B
Binding to proteins usually induces perturbation of nuclear magnetic...
Probing the active conformation of FGLamide allatostatin analogs with N-terminal modifications using NMR spectroscopy and molecular modeling.
Linear Mode
