Related Articles1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5.
Biochemistry. 1990 Oct 16;29(41):9623-31
Authors: Lee KB, La Mar GN, Kehres LA, Fujinari EM, Smith KM, Pochapsky TC, Sligar SG
The proton nuclear magnetic resonance spectra of the soluble fragment of native bovine and genetically engineered wild-type rat ferricytochrome b5 reconstituted with a wide variety of hemes chemically modified at 2- and/or 4-positions have been recorded and analyzed. While all but one nonsymmetric heme yielded comparable amounts of the two heme orientations immediately after reconstitution, the relative proportion of the two orientations at equilibrium varied widely. The unpaired spin density distribution in the heme pi system leads to substituent hyperfine shift patterns in these paramagnetic complexes that are completely diagnostic of the heme orientation in the protein matrix. An empirical assignment strategy is outlined and applied which allows unequivocal assignment of the absolute orientation of a derivatized heme within the protein matrix. Using a series of hemes lacking 2-fold symmetry solely due to a single substitution, the preferences for localized site occupation of vinyls, methyls, and hydrogens are developed. The large differences in relative stability of the two orientations of native protohemin in the two cytochromes b5 is shown to result from the additivity of localized effects for the bovine protein and the near cancellation of competing effects in the rat protein. The major determinant of the heme orientation is judged to be a repulsive interaction between a vinyl and a hydrophobic cluster of amino acids including positions 23 and 25. The differences in this heme orientational preference among bovine, rat, and chicken ferricytochromes b5 could be correlated with the relative steric bulk of the residues at positions 23 and 25.(ABSTRACT TRUNCATED AT 250 WORDS)
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Biochemistry. 2011 Aug 27;
Authors: Peng D, Satterlee JD, Ma LH, Dallas JL, Smith KM, Zhang X, Sato M, La Mar GN
Abstract
Heme oxygenase, HO, from the pathogenic bacterium N. meningitidis, NmHO, which...
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Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
Methanol Strengthens Hydrogen Bonds and Weakens Hydrophobic Interactions in Proteins - A Combined Molecular Dynamics and NMR study.
J Phys Chem B. 2011 May 2;
Authors: Hwang S, Shao Q, Williams H, Hilty C, Gao YQ
A combined simulation and experimental study was performed to investigate how methanol affects the structure of a model peptide BBA5. BBA5 forms a stable ?-hairpin-?-helix structure in aqueous solutions....
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[NMR paper] 1H and 13C NMR investigation of the influence of nonligated residue contacts on the h
1H and 13C NMR investigation of the influence of nonligated residue contacts on the heme electronic structure in cyanometmyoglobin complexes reconstituted with centro- and pseudocentrosymmetric hemins.
Related Articles 1H and 13C NMR investigation of the influence of nonligated residue contacts on the heme electronic structure in cyanometmyoglobin complexes reconstituted with centro- and pseudocentrosymmetric hemins.
J Am Chem Soc. 2001 Oct 17;123(41):10063-70
Authors: Hu B, Hauksson JB, Tran AT, Kolczak U, Pandey RK, Rezzano IN, Smith KM, La Mar GN
...
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[NMR paper] Solution (1)H NMR study of the influence of distal hydrogen bonding and N terminus ac
Solution (1)H NMR study of the influence of distal hydrogen bonding and N terminus acetylation on the active site electronic and molecular structure of Aplysia limacina cyanomet myoglobin.
Related Articles Solution (1)H NMR study of the influence of distal hydrogen bonding and N terminus acetylation on the active site electronic and molecular structure of Aplysia limacina cyanomet myoglobin.
J Biol Chem. 2000 Jan 14;275(2):742-51
Authors: Nguyen BD, Xia Z, Cutruzzolá F, Allocatelli CT, Brunori M, La Mar GN
The sea hare Aplysia limacina...
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[NMR paper] Secondary structure in solution of the hydrophobic protein of soybean (HPS) as reveal
Secondary structure in solution of the hydrophobic protein of soybean (HPS) as revealed by 1H NMR.
Related Articles Secondary structure in solution of the hydrophobic protein of soybean (HPS) as revealed by 1H NMR.
J Biomol Struct Dyn. 1995 Apr;12(5):1009-22
Authors: Sodano P, Ptak M
COSY, TOCSY and NOESY experiments have been used to assign sequentially the 1H 500 MHz NMR spectra of the Hydrophobic Protein of Soybean (HPS). Spin systems identification combined with sequential assignment allowed to identify the proton resonances of this 80...
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[NMR paper] Demonstration of positionally disordered water within a protein hydrophobic cavity by
Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR.
Related Articles Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR.
Science. 1995 Mar 24;267(5205):1813-7
Authors: Ernst JA, Clubb RT, Zhou HX, Gronenborn AM, Clore GM
The presence and location of water of hydration (that is, bound water) in the solution structure of human interleukin-1 beta (hIL-1 beta) was investigated with water-selective two-dimensional heteronuclear magnetic resonance spectroscopy. It is shown...
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[NMR paper] Dynamic DNA contacts observed in the NMR structure of winged helix protein-DNA comple
Dynamic DNA contacts observed in the NMR structure of winged helix protein-DNA complex.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Dynamic DNA contacts observed in the NMR structure of winged helix protein-DNA complex.
J Mol Biol. 1999 Jun 18;289(4):683-90
Authors: Jin C, Marsden I, Chen X, Liao X
Genesis is an HNF-3/fkh homologous protein. By using multi-dimensional NMR techniques, we have obtained the solution structure and backbone dynamics of Genesis complexed...
1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group rec
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