Related ArticlesHeteronuclear solution-state NMR studies of the chromophore in cyanobacterial phytochrome Cph1.
Biochemistry. 2005 Jun 14;44(23):8244-50
Authors: Strauss HM, Hughes J, Schmieder P
Precise structural information regarding the chromophore binding pocket is essential for an understanding of photochromicity and photoconversion in phytochrome photoreceptors. To this end, we are studying the 59 kDa N-terminal module of the cyanobacterial phytochrome Cph1 from Synechocystis sp. PCC 6803 in both thermally stable forms (Pr and Pfr) using solution-state NMR spectroscopy. The protein is deuterated, while the chromophore, phycocyanobilin (PCB), is isotopically labeled with (15)N or (13)C and (15)N. We have established a simple approach for preparing labeled PCB based on BG11 medium supplemented with an appropriate buffer and NaH(13)CO(3) and Na(15)NO(3) as sole carbon and nitrogen sources, respectively. We show that structural details of the chromophore binding pocket in both Pr and Pfr forms can be obtained using multidimensional heteronuclear solution-state NMR spectroscopy. Using one-dimensional (15)N NMR spectra, we show unequivocally that the chromophore is protonated in both Pr and Pfr states.
Ruthenium Agostic (Phosphinoaryl)borane Complexes: Multinuclear Solid-State and Solution NMR, X-ray, and DFT Studies
Ruthenium Agostic (Phosphinoaryl)borane Complexes: Multinuclear Solid-State and Solution NMR, X-ray, and DFT Studies
Yann Gloaguen, Gilles Alcaraz, Alban S. Petit, Eric Clot, Yannick Coppel, Laure Vendier and Sylviane Sabo-Etienne
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203828r/aop/images/medium/ja-2011-03828r_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203828r
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/extLacz2EPY
nmrlearner
Journal club
0
10-11-2011 06:32 AM
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Biophys J. 2011 Sep 7;101(5):1193-201
Authors: Park TJ, Kim JS, Ahn HC, Kim Y
Abstract
Lactophoricin (LPcin-I) is an antimicrobial, amphiphatic, cationic peptide with 23-amino acid residues isolated from bovine milk. Its analogous peptide, LPcin-II, lacks six N-terminal amino acids compared to LPcin-I. Interestingly, LPcin-II does not display any...
nmrlearner
Journal club
0
09-06-2011 06:02 PM
Solution- and solid-state NMR studies of GPCRs and their ligands (Review).
Solution- and solid-state NMR studies of GPCRs and their ligands (Review).
Related Articles Solution- and solid-state NMR studies of GPCRs and their ligands (Review).
Biochim Biophys Acta. 2010 Oct 14;
Authors: Tapaneeyakorn S, Goddard AD, Oates J, Willis CL, Watts A
G protein-coupled receptors (GPCRs) represent one of the major targets of new drugs on the market given their roles as key membrane receptors in many cellular signalling pathways. Structure-based drug design has potential to be the most reliable method for novel drug discovery....
nmrlearner
Journal club
0
10-19-2010 04:51 PM
[NMR paper] Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte c
Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer.
Biochemistry. 1996 May 28;35(21):6569-84
Authors: Handel TM, Domaille PJ
A full high-resolution three-dimensional solution structure of the monocyte chemoattractant protein-1 (MCP-1 or MCAF)...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] The solution structure of bovine ferricytochrome b5 determined using heteronuclear NM
The solution structure of bovine ferricytochrome b5 determined using heteronuclear NMR methods.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The solution structure of bovine ferricytochrome b5 determined using heteronuclear NMR methods.
J Mol Biol. 1996 Apr 26;258(1):172-89
Authors: Muskett FW, Kelly GP, Whitford D
The solution structure of a recombinant form of cytochrome b5 containing 104 amino acid residues has been determined using three-dimensional NMR...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and
Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.
Related Articles Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.
Biochemistry. 1994 Mar 29;33(12):3515-31
Authors: Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED
A high-resolution solution structure of the GDP form of a truncated version of the ras p21 protein (residues 1-166) has been determined using NMR spectroscopy. Ras p21 is the...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and
Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.
Related Articles Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.
Biochemistry. 1994 Mar 29;33(12):3515-31
Authors: Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED
A high-resolution solution structure of the GDP form of a truncated version of the ras p21 protein (residues 1-166) has been determined using NMR spectroscopy. Ras p21 is the...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] Structures of larger proteins in solution: three- and four-dimensional heteronuclear
Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy.
Related Articles Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy.
Science. 1991 Jun 7;252(5011):1390-9
Authors: Clore GM, Gronenborn AM
Three- and four-dimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy offers dramatic improvements in spectral resolution by spreading through-bond and through-space correlations in three and four orthogonal frequency axes....