Related ArticlesExpression and secondary structure determination by NMR methods of the major house dust mite allergen Der p 2.
J Biol Chem. 1997 Oct 24;272(43):26893-8
Authors: Mueller GA, Smith AM, Williams DC, Hakkaart GA, Aalberse RC, Chapman MD, Rule GS, Benjamin DC
There exists a strong correlation between asthma and sensitization to indoor allergens. This study reports on the secondary structure of the major house dust mite allergen Der p 2, determined using heteronuclear NMR methods. The DNA was subcloned from the yeast expression vector pSAY1 into the high yield bacterial expression vector pET21a, resulting in yields of 50 mg/liter. The recombinant protein was shown to have immunoreactivity comparable with that of the natural mite protein using competitive inhibition enzyme-linked immunosorbent assay (ELISA) and a modified monoclonal radioallergosorbent test (RAST). The secondary structure was determined by examining chemical shifts, short and long range NOESYs, JHN-HA coupling constants, and amide exchange rates. From these data, it is clear that Der p 2 is composed of beta-sheets and random coil. Based on long range distance constraints, a number of beta-strands were aligned into two three-stranded, anti-parallel beta-sheets.
[Optimization of the methods for small peptide solution structure determination by NMR spectroscopy].
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Mol Biol (Mosk). 2010 Nov-Dec;44(6):1075-85
Authors:
NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints from NMR spectra. At the same time, short charged peptides play an important role in a number of biological processes, in particular in pathogenesis of neurodegenerative...
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[NMR paper] Multidimensional NMR methods for protein structure determination.
Multidimensional NMR methods for protein structure determination.
Related Articles Multidimensional NMR methods for protein structure determination.
IUBMB Life. 2001 Dec;52(6):291-302
Authors: Kanelis V, Forman-Kay JD, Kay LE
Structural studies of proteins are critical for understanding biological processes at the molecular level. Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique for obtaining structural and dynamic information on proteins and protein-ligand complexes. In the present review, methodologies for NMR structure...
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[NMR paper] Secondary structure determination by NMR spectroscopy of an immunoglobulin-like domai
Secondary structure determination by NMR spectroscopy of an immunoglobulin-like domain from the giant muscle protein titin.
Related Articles Secondary structure determination by NMR spectroscopy of an immunoglobulin-like domain from the giant muscle protein titin.
J Biomol NMR. 1995 Jul;6(1):48-58
Authors: Pfuhl M, Gautel M, Politou AS, Joseph C, Pastore A
We present the complete 15N and 1H NMR assignment and the secondary structure of an immunoglobulin-like domain from the giant muscle protein titin. The assignment was obtained using...
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[NMR paper] An RBD that does not bind RNA: NMR secondary structure determination and biochemical
An RBD that does not bind RNA: NMR secondary structure determination and biochemical properties of the C-terminal RNA binding domain from the human U1A protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles An RBD that does not bind RNA: NMR secondary structure determination and biochemical properties of the C-terminal RNA binding domain from the human U1A protein.
J Mol Biol. 1995 Apr 7;247(4):739-52
Authors: Lu J, Hall KB
We have obtained backbone 1H, 15N, and 13C...
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[NMR paper] NMR determination of the secondary structure and the three-dimensional polypeptide ba
NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.
FEBS Lett. 1993 Nov 29;335(1):18-26
Authors: Szyperski T, Scheek S, Johansson J, Assmann G, Seedorf U, Wüthrich K
Nuclear magnetic resonance (NMR)...
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[NMR paper] A systematic comparison of three structure determination methods from NMR data: depen
A systematic comparison of three structure determination methods from NMR data: dependence upon quality and quantity of data.
Related Articles A systematic comparison of three structure determination methods from NMR data: dependence upon quality and quantity of data.
J Biomol NMR. 1992 Jul;2(4):373-88
Authors: Liu Y, Zhao D, Altman R, Jardetzky O
We have systematically examined how the quality of NMR protein structures depends on (1) the number of NOE distance constraints, (2) their assumed precision, (3) the method of structure calculation...
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Combining NMR and EPR Methods for Homodimer Protein Structure Determination.
Combining NMR and EPR Methods for Homodimer Protein Structure Determination.
Related Articles Combining NMR and EPR Methods for Homodimer Protein Structure Determination.
J Am Chem Soc. 2010 Aug 10;
Authors: Yang Y, Ramelot TA, McCarrick RM, Ni S, Feldmann EA, Cort JR, Wang H, Ciccosanti C, Jiang M, Janjua H, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA
There is a general need to develop more powerful and more robust methods for structural characterization of homodimers, homo-oligomers, and multiprotein complexes using...
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Combining NMR and EPR Methods for Homodimer Protein Structure Determination
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja105080h/aop/images/medium/ja-2010-05080h_0003.gif
Combining NMR and EPR Methods for Homodimer Protein Structure Determination
There is a general need to develop more powerful and more robust methods for structural characterization of homodimers, homo-oligomers, and multiprotein complexes using solution-state NMR methods. In recent years, there has been increasing emphasis on integrating distinct and complementary methodologies for structure determination of multiprotein ...