Exploring NMR ensembles of calcium binding proteins: perspectives to design inhibitors of protein-protein interactions.
Exploring NMR ensembles of calcium binding proteins: perspectives to design inhibitors of protein-protein interactions.
Exploring NMR ensembles of calcium binding proteins: perspectives to design inhibitors of protein-protein interactions.
BMC Struct Biol. 2011 May 12;11(1):24
Authors: Isvoran A, Badel A, Craescu CT, Miron S, Miteva MA
ABSTRACT: BACKGROUND: Disrupting protein-protein interactions by small organic molecules is nowadays a promising strategy employed to block protein targets involved in different pathologies. However, structural...
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05-17-2011 06:21 PM
Exploring NMR ensembles of calcium binding proteins: perspectives to design ... - 7thSpace Interactive (press release)
Exploring NMR ensembles of calcium binding proteins: perspectives to design ... - 7thSpace Interactive (press release)
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Exploring NMR ensembles of calcium binding proteins: perspectives to design ...
7thSpace Interactive (press release)
We employed several scoring methods in order to find the best protein conformations. Our results show that docking on NMR structures of calmodulin and centrin can be very helpful to take into account conformational changes occurring at protein-protein ...
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05-13-2011 07:41 AM
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a m
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system.
Related Articles Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system.
Prog Nucl Magn Reson Spectrosc. 2010 May;56(4):346-59
Authors: Kato K, Yamaguchi Y, Arata Y
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10-19-2010 04:51 PM
[BMNRC community] Perspectives on NMR in drug discovery: a technique comes of age
Perspectives on NMR in drug discovery: a technique comes of age
http://www.nature.com/nrd/journal/v7/n9/abs/nrd2606.html
Nature Reviews Drug Discovery 7, 738-745 (September 2008) | doi:10.1038/nrd2606
Go to BMNRC community to find more info about this topic.
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09-02-2010 04:59 AM
[NMR paper] NMR and crystallography--complementary approaches to structure determination.
NMR and crystallography--complementary approaches to structure determination.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR and crystallography--complementary approaches to structure determination.
Trends Biotechnol. 1994 May;12(5):149-53
Authors: MacArthur MW, Driscoll PC, Thornton JM
A knowledge of the three-dimensional structure of a protein is essential to understand how a protein performs its functions. It is also a prime requirement for the rational design...
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08-22-2010 03:33 AM
[NMR paper] NMR and crystallography--complementary approaches to structure determination.
NMR and crystallography--complementary approaches to structure determination.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR and crystallography--complementary approaches to structure determination.
Trends Biotechnol. 1994 May;12(5):149-53
Authors: MacArthur MW, Driscoll PC, Thornton JM
A knowledge of the three-dimensional structure of a protein is essential to understand how a protein performs its functions. It is also a prime requirement for the rational design...
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08-22-2010 03:33 AM
[NMR paper] 1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 k
1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 kDa.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 kDa.
Int J Biol Macromol. 1994 Oct;16(5):227-35
Authors: Gettins PG
The three-dimensional solution structures of proteins larger than about 25 kDa cannot at present be determined by multi-dimensional nuclear magnetic resonance (NMR) methods. However,...
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08-22-2010 03:29 AM
Approaches to the assignment of 19F resonances from 3-fluorophenylalanine labeled cal
Abstract Traditional single site replacement mutations (in this case, phenylalanine to tyrosine) were compared with methods which exclusively employ 15N and 19F-edited two- and three-dimensional NMR experiments for purposes of assigning 19F NMR resonances from calmodulin (CaM), biosynthetically labeled with 3-fluorophenylalanine (3-FPhe). The global substitution of 3-FPhe for native phenylalanine was tolerated in CaM as evidenced by a comparison of 1H-15N HSQC spectra and calcium binding assays in the presence and absence of 3-FPhe. The 19F NMR spectrum reveals six resolved resonances, one...