Related ArticlesSolution structure determination by NMR spectroscopy of a synthetic peptide corresponding to a putative amphipathic alpha-helix of spiralin: resonance assignment, distance geometry and simulated annealing.
Biochim Biophys Acta. 1995 May 4;1235(2):169-77
Authors: Bondon A, Berthault P, Segalas I, Perly B, Wróblewski H
Spiralin is the major protein of the plasma membrane of several spiroplasmas. Neither the function of this protein nor the crystallographic structure is known. Analysis of the primary structure of spiralin from Spiroplasma melliferum BC3 suggests the presence of an amphipathic peptide in the 143-162 region (Chevalier, C., Saillard, C. and Bové, J.M. (1990) J. Bacteriol. 172, 6090-6097). The structure of a synthetic peptide, H2N-L-N-A-V-N-T-Y-A-T-L-A-K-A-V-L-D-A-I-Q-N-amide, corresponding to this fragment has been examined by 1H-NMR spectroscopy. This 20 amino acid peptide adopts a random coil structure in solution, but the addition of trifluoroethanol stabilizes a structure exhibiting alpha-helical character. The 1H-NMR spectrum has been fully assigned in CF3CD2OD/H2O (30:70, v/v) and the three-dimensional structure has been elucidated using NMR-derived distance information. The calculated structures have been obtained by dynamical simulated annealing or distance geometry followed by simulated annealing. Both sets of structures have been energy-minimized using CHARMm potential. The resulting structures are very similar in terms of constraint violations and energies. It is demonstrated that whereas the first three residues exhibit a large flexibility, the remaining sequence is helical.
[Optimization of the methods for small peptide solution structure determination by NMR spectroscopy].
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Mol Biol (Mosk). 2010 Nov-Dec;44(6):1075-85
Authors:
NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints from NMR spectra. At the same time, short charged peptides play an important role in a number of biological processes, in particular in pathogenesis of neurodegenerative...
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[NMR paper] Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent pro
Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
Related Articles Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
J Pept Res. 1997 Mar;49(3):210-20
Authors: Padilla A, Hauer JA, Tsigelny I, Parello J, Taylor SS
Peptides derived from the inhibitor of cAMP-dependent protein kinase. PKI, have been studied by 2D 1H NMR techniques. These include the inhibitor...
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[NMR paper] Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent pro
Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
Related Articles Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
J Pept Res. 1997 Mar;49(3):210-20
Authors: Padilla A, Hauer JA, Tsigelny I, Parello J, Taylor SS
Peptides derived from the inhibitor of cAMP-dependent protein kinase. PKI, have been studied by 2D 1H NMR techniques. These include the inhibitor...
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08-22-2010 03:03 PM
[NMR paper] The solution structure of the synthetic circular peptide CGVSRQGKPYC. NMR studies of
The solution structure of the synthetic circular peptide CGVSRQGKPYC. NMR studies of the folding of a synthetic model for the DNA-binding loop of the ssDNA-binding protein encoded by gene V of phage M13.
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 The solution structure of the synthetic circular peptide CGVSRQGKPYC. NMR studies of the folding of a synthetic model for the DNA-binding loop of the ssDNA-binding protein encoded by gene V of phage M13.
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[NMR paper] Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy.
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy.
J Mol Biol. 1995 Jun 2;249(2):441-62
Authors: Skelton NJ, Kördel J, Chazin WJ
The three-dimensional structure of apo calbindin D9k has been determined using constraints generated from nuclear magnetic resonance spectroscopy. The family of solution structures...
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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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08-22-2010 03:33 AM
[NMR paper] Determination of the solution structure of a synthetic two-site calcium-binding homod
Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.
Related Articles Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.
Biochemistry. 1992 Oct 13;31(40):9572-80
Authors: Shaw GS, Hodges RS, Sykes BD
The solution structure of a 34-residue synthetic calcium-binding peptide from site III of chicken troponin-C has been determined by 1H NMR spectroscopy. In solution and in the presence of calcium...
Solution structure determination by NMR spectroscopy of a synthetic peptide correspon
Linear Mode
