Related ArticlesMultidimensional 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 determination of proteins and macromolecular complexes are described. In addition, a number of recent advances that reduce the molecular weight limitations previously imposed on NMR studies of biomolecules are discussed, highlighting applications of these technologies to protein systems studied in our laboratories.
[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] NMR methods for the determination of protein-ligand dissociation constants.
NMR methods for the determination of protein-ligand dissociation constants.
Related Articles NMR methods for the determination of protein-ligand dissociation constants.
Curr Top Med Chem. 2003;3(1):39-53
Authors: Fielding L
This article is a review with 83 references of the application of NMR to the measurement of the dissociation constants of protein-ligand complexes. After briefly discussing some general concepts of molecular stability, the text turns to consider which NMR parameters are reporters of complex formation. The available data...
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[NMR paper] Expression and secondary structure determination by NMR methods of the major house du
Expression and secondary structure determination by NMR methods of the major house dust mite allergen Der p 2.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Expression 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...
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[NMR900 blog] Multidimensional NMR Methods for the Solution State
Multidimensional NMR Methods for the Solution State
edited by Gareth A. Morris and James W. Emsley
Hardcover: 580 pages
Publisher: Wiley; June 2010
Language: English
ISBN: 978-0470770757
http://www.amazon.com/dp/0470770759
http://www.amazon.ca/dp/0470770759
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08-22-2010 02:30 AM
[NMR900 blog] Multidimensional NMR Methods for the Solution State
Multidimensional NMR Methods for the Solution State
edited by Gareth A. Morris and James W. Emsley
Hardcover: 580 pages
Publisher: Wiley; June 2010
Language: English
ISBN: 978-0470770757
http://www.amazon.com/dp/0470770759
http://www.amazon.ca/dp/0470770759
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08-22-2010 02:18 AM
[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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08-21-2010 11:41 PM
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 ...