Related ArticlesInfluence of the extent of branching on solution conformations of complex oligosaccharides: a molecular dynamics and NMR study of a penta-antennary "bisected" N-glycan.
Biochemistry. 1995 Oct 31;34(43):14131-7
Authors: Rutherford TJ, Neville DC, Homans SW
The solution conformation of an agalactosyl penta-antennary "bisected" N-linked glycan from hen ovomucoid has been determined using a combination of 1H-NMR NOE measurements and restrained molecular dynamics (MD) simulations. The majority of glycosidic linkages exhibited restricted torsional fluctuations about the global minimum energy configuration, of an extent which was generally less than that observed in N-linked glycans with a smaller number of antennae. The locations of terminal galactose residues in the native glycan, which exhibit branch specificity, could not readily be rationalized in terms of relative accessibility by the relevant galactosyltransferase of the various nonreducing terminal 2-acetamido-2-deoxy-D-glucopyranose (GlcNAc) residues in the agalactosyl glycan, suggesting either that the parent protein exhibits substantial control over glycosylation or that more than one transferase is responsible for galactosylation.
[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] Determination of solution conformations of PrP106-126, a neurotoxic fragment of prion
Determination of solution conformations of PrP106-126, a neurotoxic fragment of prion protein, by 1H NMR and restrained molecular dynamics.
Related Articles Determination of solution conformations of PrP106-126, a neurotoxic fragment of prion protein, by 1H NMR and restrained molecular dynamics.
Eur J Biochem. 1999 Dec;266(3):1192-201
Authors: Ragg E, Tagliavini F, Malesani P, Monticelli L, Bugiani O, Forloni G, Salmona M
Experimental two-dimensional 1H NMR data have been obtained for PrP106-128 under the following solvent conditions:...
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[NMR paper] The solution conformations of amino acids from molecular dynamics simulations of Gly-
The solution conformations of amino acids from molecular dynamics simulations of Gly-X-Gly peptides: comparison with NMR parameters.
Related Articles The solution conformations of amino acids from molecular dynamics simulations of Gly-X-Gly peptides: comparison with NMR parameters.
Biochem Cell Biol. 1998;76(2-3):164-70
Authors: van der Spoel D
The conformations that amino acids can adopt in the random coil state are of fundamental interest in the context of protein folding research and studies of protein-peptide interactions. To date, no...
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[NMR paper] Comparison of the solution conformations of a human immunodeficiency virus peptidomim
Comparison of the solution conformations of a human immunodeficiency virus peptidomimetic and its retro-inverso isomer using 1H NMR spectroscopy.
Related Articles Comparison of the solution conformations of a human immunodeficiency virus peptidomimetic and its retro-inverso isomer using 1H NMR spectroscopy.
J Pept Res. 1997 Dec;50(6):421-35
Authors: Higgins KA, Bicknell W, Keah HH, Hearn MT
The solution conformations of the all L-alpha-peptide 1 and the corresponding retro-all D-alpha-peptide 2, two 20-metric peptides which generate antibodies...
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[NMR paper] Solution conformations of proline rings in proteins studied by NMR spectroscopy.
Solution conformations of proline rings in proteins studied by NMR spectroscopy.
Related Articles Solution conformations of proline rings in proteins studied by NMR spectroscopy.
J Biomol NMR. 1995 Sep;6(2):123-8
Authors: Cai M, Huang Y, Liu J, Krishnamoorthi R
Three different conformations of proline rings in a protein in solution, Up, Down and Twist, have been distinguished, and stereospecific assignments of the pyrrolidine beta-, gamma- and delta-hydrogens have been made on the basis of 1H-1H vicinal coupling constant patterns and...
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[NMR paper] NMR-derived solution conformations of a hybrid synthetic peptide containing multiple
NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
Related Articles NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
Biochemistry. 1994 Mar 1;33(8):2055-62
Authors: de Lorimier R, Moody MA, Haynes BF, Spicer LD
Solution conformations of a 40-residue hybrid peptide containing T-helper epitopes and B-cell...
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[NMR paper] NMR-derived solution conformations of a hybrid synthetic peptide containing multiple
NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
Related Articles NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
Biochemistry. 1994 Mar 1;33(8):2055-62
Authors: de Lorimier R, Moody MA, Haynes BF, Spicer LD
Solution conformations of a 40-residue hybrid peptide containing T-helper epitopes and B-cell...
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[NMR paper] Comparison of protein structures in solution using local conformations derived from N
Comparison of protein structures in solution using local conformations derived from NMR data: application to cytochrome c.
Related Articles Comparison of protein structures in solution using local conformations derived from NMR data: application to cytochrome c.
J Biomol Struct Dyn. 1994 Dec;12(3):527-58
Authors: Kar L, Sherman SA, Johnson ME
Structural comparisons of proteins in solution are often required to examine structure-functional relationships, study structural effects of mutations or distinguish between various forms of the same...