Related ArticlesA NMR investigation on the interactions of the alpha-oligomeric form of the M13 coat protein with lipids, which mimic the Escherichia coli inner membrane.
Biochim Biophys Acta. 1991 Jul 1;1066(1):102-8
Authors: Sanders JC, Poile TW, Spruijt RB, Van Nuland NA, Watts A, Hemminga MA
The interaction of the M13 bacteriophage major coat protein in the alpha-oligomeric form with specifically deuterated phospholipid headgroups which mimic the Escherichia coli inner membrane, has been studied using NMR methods. As can be seen from the deuterium NMR spectra obtained with headgroup trimethyl deuterated DOPC, the coat protein in the alpha-oligomeric form does not give rise to trapped lipids as observed with M13 coat protein in the beta-polymeric form (Van Gorkom et al. (1990) Biochemistry 29, 3828-3834). The quadrupolar splittings of the alpha headgroup methylene deuterons of deuterated phosphatidylcholine and phosphatidylethanolamine decrease, whereas the quadrupolar splittings of the beta headgroup methylene deuterons of the two lipids increase with increasing protein content. All deuterated segments in the phosphatidylglycerol headgroup show the same relative decrease of the NMR quadrupolar splittings. These results are interpreted in terms of a change in torsion angles of the methylene groups, induced by positive charges, probably lysine residues of the protein at the membrane surface. For all lipid bilayer compositions studied the head-group perturbations are similar. It is concluded that there is no strong specific interaction between one of the lipid types examined and the M13 coat protein. From the spin-spin (T2e) relaxation time and spin-lattice (T1z) relaxation time of all deuterated lipids it is concluded that at the bilayer surface only slow motions are affected by the M13 coat protein.
[NMR paper] Probing the oligomeric state of phospholamban variants in phospholipid bilayers from
Probing the oligomeric state of phospholamban variants in phospholipid bilayers from solid-state NMR measurements of rotational diffusion rates.
Related Articles Probing the oligomeric state of phospholamban variants in phospholipid bilayers from solid-state NMR measurements of rotational diffusion rates.
Biochemistry. 2005 Mar 15;44(10):4055-66
Authors: Hughes E, Clayton JC, Middleton DA
Phospholamban (PLB) is a small transmembrane protein that regulates calcium transport across the sarcoplasmic reticulum (SR) of cardiac cells. PLB...
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[NMR paper] Solution-state NMR investigation of DNA binding interactions in Escherichia coli form
Solution-state NMR investigation of DNA binding interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): a dynamic description of the DNA/protein interface.
Related Articles Solution-state NMR investigation of DNA binding interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): a dynamic description of the DNA/protein interface.
DNA Repair (Amst). 2005 Mar 2;4(3):327-39
Authors: Buchko GW, McAteer K, Wallace SS, Kennedy MA
Formamidopyrimidine-DNA glycosylase (Fpg) is a base excision repair (BER) protein...
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[NMR paper] Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble
Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.
Related Articles Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.
J Am Chem Soc. 2005 Jan 19;127(2):476-7
Authors: Dedmon MM, Lindorff-Larsen K, Christodoulou J, Vendruscolo M, Dobson CM
The intrinsically disordered protein alpha-synuclein plays a key role in the pathogenesis of Parkinson's disease (PD). We show here that the native state of alpha-synuclein...
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[NMR paper] Dissecting structural and electrostatic interactions of charged groups in alpha-sarci
Dissecting structural and electrostatic interactions of charged groups in alpha-sarcin. An NMR study of some mutants involving the catalytic residues.
Related Articles Dissecting structural and electrostatic interactions of charged groups in alpha-sarcin. An NMR study of some mutants involving the catalytic residues.
Biochemistry. 2003 Nov 18;42(45):13122-33
Authors: García-Mayoral MF, Pérez-Cañadillas JM, Santoro J, Ibarra-Molero B, Sanchez-Ruiz JM, Lacadena J, Martínez del Pozo A, Gavilanes JG, Rico M, Bruix M
The cytotoxic ribonuclease...
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[NMR paper] Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined b
Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR.
Related Articles Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR.
Protein Sci. 1998 Sep;7(9):1930-8
Authors: Kim S, Baum J
alpha-Lactalbumin (alpha-LA) undergoes a pH-dependent unfolding from the native state to a partially unfolded state (the molten globule state). To understand the role of electrostatic interactions in protein denaturation, NMR and CD pH titration experiments are performed on guinea pig...
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[NMR paper] NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and c
NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Related Articles NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Int J Biol Macromol. 1998 May-Jun;22(3-4):197-209
Authors: Carver JA, Lindner RA
The subunit molecular mass of alpha-crystallin, like many small heat-shock proteins (sHsps), is around 20 kDa although the protein exists as a large aggregate of average mass around 800...
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Oligomeric Structure of a Cathelicidin Antimicrobial Peptide in Dodecylphosphocholine
Oligomeric Structure of a Cathelicidin Antimicrobial Peptide in Dodecylphosphocholine Micelle Determined by NMR Spectroscopy.
Related Articles Oligomeric Structure of a Cathelicidin Antimicrobial Peptide in Dodecylphosphocholine Micelle Determined by NMR Spectroscopy.
Biochim Biophys Acta. 2010 Oct 6;
Authors: Saravanan R, Bhattacharjya S
The broad spectrum of antibacterial activities of host defense cationic antimicrobial peptides (AMPs) arises from their ability to perturb membrane integrity of the microbes. The mechanisms are often thought to...
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[NMR paper] Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotei
Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus. A study by 13C magic angle spinning NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus. A study by 13C magic angle spinning NMR.
FEBS Lett. 1995 Mar 27;362(1):34-8
Authors: Weesie RJ, Askin D, Jansen FJ, de...
A NMR investigation on the interactions of the alpha-oligomeric form of the M13 coat
Linear Mode
