Related ArticlesStudy of electrostatic potential surface distribution of wild-type plastocyanin Synechocystis solution structure determined by homonuclear NMR.
Biopolymers. 2003 Oct;70(2):212-20
Authors: Monleķn D, Celda B
Plastocyanin is a small (approximately 10 kDa), type I blue copper protein that works as an electron donor to photosystem I from cytochrome f in both chloroplast systems and in some strains of cyanobacteria. Comparative studies of the kinetic mechanisms of plastocyanins in different organisms show that the electron transfer from photosystem I happens by simple collision in cyanobacteria but through a intermediate transition complex in green algae and superior plants. Previous work has proved that this effect cannot be explained by structural variations across the different plastocyanins but it can be explained by differences in the electrostatic potential distribution at the protein surface. In that case, minor conformational errors at the amino acid side chain level may imply an important effect in the electrostatic potential distribution calculation. In this work we present a high resolution study of side chain conformation by homonuclear NMR for the reduced wild-type plastocyanin Synechocystis using intensity ratios for 2D-NOESY and 2D-H,H-TOCSY cross peaks at different mixing times. We also present the corresponding comparison with different plastocyanin structures and the effect in the electrostatic potential distribution at the protein surface. We discuss the importance of indirect J-coupling information from TOCSY-type experiments as complement for intraresidue distances derived from NOESY experiments in the determination of side chain orientation and stereo-specific assignments.
An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant.
An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant.
An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant.
Proteins. 2011 May 16;
Authors: Gayen S, Li Q, Chen AS, Nguyen TH, Huang Q, Hill J, Kang C
The human Ether-ā-go-go Related Gene (hERG) potassium channel plays an important role in the heart by controlling the rapid delayed rectifier current. The N-terminal 135 residues (NTD) contain a Per-Arnt-Sim (PAS) domain and an N-terminal amphipathic helix....
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Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via (13)C-(15)N dynamic REDOR NMR.
Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via (13)C-(15)N dynamic REDOR NMR.
Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via (13)C-(15)N dynamic REDOR NMR.
Solid State Nucl Magn Reson. 2011 Mar 23;
Authors: Mao Y, Jeong M, Wang T, Ba Y
Antifreeze proteins (AFPs) provide survival mechanism for species living in subzero environments by lowering the freezing points of their...
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[NMR paper] Molecular insight into the electrostatic membrane surface potential by 14n/31p MAS NM
Molecular insight into the electrostatic membrane surface potential by 14n/31p MAS NMR spectroscopy: nociceptin-lipid association.
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J Am Chem Soc. 2005 May 11;127(18):6610-6
Authors: Lindström F, Williamson PT, Gröbner G
Exploiting naturally abundant (14)N and (31)P nuclei by high-resolution MAS NMR (magic angle spinning nuclear magnetic resonance) provides a molecular view of the electrostatic...
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[NMR paper] 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-
13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.
Biophys J. 1994 Jun;66(6):2111-26
Authors: Kemple MD, Yuan...
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[NMR paper] 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-
13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.
Biophys J. 1994 Jun;66(6):2111-26
Authors: Kemple MD, Yuan...
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[NMR paper] 31P and 13C NMR spectroscopic study of wild type and multidrug resistant Ehrlich asci
31P and 13C NMR spectroscopic study of wild type and multidrug resistant Ehrlich ascites tumor cells.
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Oncol Res. 1993;5(3):119-26
Authors: Rasmussen J, Hansen LL, Friche E, Jaroszewski JW
Steady-state 31P NMR spectra of wild type EHR2 Ehrlich ascites tumor cells and multidrug resistant EHR2/DNR+ cells, immobilized in agarose threads, and continuously perfused with medium, showed temperature-dependent differences in the levels...
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[NMR paper] Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
Eur J Biochem. 1991 Aug 15;200(1):139-48
Authors: Folkers PJ, Stassen AP, van Duynhoven JP, Harmsen BJ, Konings RN, Hilbers CW
Recording of good quality NMR spectra of the single-stranded DNA binding protein gene V of the...
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[NMR paper] Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
Eur J Biochem. 1991 Aug 15;200(1):139-48
Authors: Folkers PJ, Stassen AP, van Duynhoven JP, Harmsen BJ, Konings RN, Hilbers CW
Recording of good quality NMR spectra of the single-stranded DNA binding protein gene V of the...