[NMR paper] Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.
Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.
Biochemistry. 2014 May 20;53(19):3106-17
Authors: Gutte PG, Jurt S, Grütter MG, Zerbe O
Abstract
The cytosolic nucleotide-binding domain and leucine-rich repeat-containing receptors (NLRs)...
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07-06-2014 08:28 PM
Unusual Structural Features Revealed by the SolutionNMR Structure of the NLRC5 Caspase Recruitment Domain
Unusual Structural Features Revealed by the SolutionNMR Structure of the NLRC5 Caspase Recruitment Domain
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi500177x/aop/images/medium/bi-2014-00177x_0007.gif
Biochemistry
DOI: 10.1021/bi500177x
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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05-09-2014 07:01 PM
[KPWU blog] [Modeller] point mutation script
point mutation script
Saw a script provided by Modeller that can quickly mutate a point to any other residues. Here is the linke <Mutate model python script by Modeller> To use the script, just type command like the following line: Example: python mutate_model.py 1t29 1699 LEU A > 1t29.log Where mutate_model.py is the script provided by Modeller 1t29 http://stats.wordpress.com/b.gif?host=kpwu.wordpress.com&blog=76132&post=812&subd=kpwu&ref=&feed=1
Go to KPWU blog to read complete post.
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11-07-2012 08:48 AM
[NMR paper] Structural characterization by NMR of the natively unfolded extracellular domain of b
Structural characterization by NMR of the natively unfolded extracellular domain of beta-dystroglycan: toward the identification of the binding epitope for alpha-dystroglycan.
Related Articles Structural characterization by NMR of the natively unfolded extracellular domain of beta-dystroglycan: toward the identification of the binding epitope for alpha-dystroglycan.
Biochemistry. 2003 Nov 25;42(46):13717-24
Authors: Bozzi M, Bianchi M, Sciandra F, Paci M, Giardina B, Brancaccio A, Cicero DO
Dystroglycan (DG) is an adhesion molecule playing a...
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11-24-2010 09:16 PM
[NMR paper] Val(659)-->Glu mutation within the transmembrane domain of ErbB-2: effects measured b
Val(659)-->Glu mutation within the transmembrane domain of ErbB-2: effects measured by (2)H NMR in fluid phospholipid bilayers.
Related Articles Val(659)-->Glu mutation within the transmembrane domain of ErbB-2: effects measured by (2)H NMR in fluid phospholipid bilayers.
Biochemistry. 2000 May 30;39(21):6572-80
Authors: Sharpe S, Barber KR, Grant CW
Certain point mutations within the hydrophobic transmembrane domains of class I receptor tyrosine kinases have been associated with oncogenic transformation in vitro and in vivo . An important...
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11-18-2010 09:15 PM
[NMR paper] Oligomerization of the EGF receptor transmembrane domain: a 2H NMR study in lipid bil
Oligomerization of the EGF receptor transmembrane domain: a 2H NMR study in lipid bilayers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Oligomerization of the EGF receptor transmembrane domain: a 2H NMR study in lipid bilayers.
Biochemistry. 1997 Oct 14;36(41):12616-24
Authors: Jones DH, Rigby AC, Barber KR, Grant CW
During the course of a previous study by wideline 2H NMR, we noted spectral features suggesting the possibility of monitoring homodimer/oligomer interactions between...
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08-22-2010 05:08 PM
[NMR paper] NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing co
NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions.
Biochemistry. 1997 Apr 1;36(13):3959-70
Authors: Zhang O, Forman-Kay JD
The isolated N-terminal SH3 domain of the Drosophila adapter protein drk (drkN SH3 domain) exists in a dynamic equilibrium between a folded (F(exch)) and an unfolded (U(exch)) state...
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08-22-2010 03:03 PM
[NMR paper] High-resolution structure of the oligomerization domain of p53 by multidimensional NM
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Related Articles High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Science. 1994 Jul 15;265(5170):386-91
Authors: Clore GM, Omichinski JG, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn AM
The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a...
Unusual Reversible Oligomerization of Unfolded DengueEnvelope Protein Domain 3 at High Temperatures and Its Abolition bya Point Mutation
Linear Mode
