Related ArticlesAssessment by 1H NMR spectroscopy of the structural behaviour of human parathyroid-hormone-related protein(1-34) and its close relationship with the N-terminal fragments of human parathyroid hormone in solution.
Biol Chem. 1997 Dec;378(12):1501-8
Authors: Gronwald W, Schomburg D, Tegge W, Wray V
Human parathyroid-hormone-related protein (hPTHrP) is a hormone that is over-expressed by a large number of tumors and is produced by a variety of normal cells. Its main biological functions are shown by the N-terminal fragment (1-34) and are similar to those of parathyroid hormone with which it shares a common G-protein-coupled receptor. Hence to gain insight into the structure-function relationship of these hormones we have investigated the solution structure of hPTHrP(1-34) in pure water alone and have monitored the effect of adding TFE. CD spectra in pure water showed that it only possesses a small content of alpha-helical secondary structure, which from the NMR data, consists of a short unstable helix between Gln-16 and Leu-24 with the rest of the peptide in an essentially unstructured state. On adding 50% TFE (v/v) there was a considerable increase in stable secondary structure, without any evidence of stable tertiary structure. The subsequent structure calculations showed the presence of two well defined helices, from Ser-3 to Gly-12 and from Asp-17 to Thr-33, connected by a flexible linker. The similarity in behaviour of hPTHrP(1-34) and the N-terminal fragments of PTH under various solution conditions is shown from the 1H NMR data presented here and an extensive review of the literature data.
[NMR paper] Rapid assessment of protein structural stability and fold validation via NMR.
Rapid assessment of protein structural stability and fold validation via NMR.
Related Articles Rapid assessment of protein structural stability and fold validation via NMR.
Methods Enzymol. 2005;394:142-75
Authors: Hoffmann B, Eichmüller C, Steinhauser O, Konrat R
In structural proteomics, it is necessary to efficiently screen in a high-throughput manner for the presence of stable structures in proteins that can be subjected to subsequent structure determination by X-ray or NMR spectroscopy. Here we illustrate that the (1)H chemical...
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[NMR paper] Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarin
Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarina probed by NMR.
Related Articles Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarina probed by NMR.
FEBS Lett. 2004 Dec 3;578(1-2):185-90
Authors: Pessanha M, Rothery EL, Louro RO, Turner DL, Miles CS, Reid GA, Chapman SK, Xavier AV, Salgueiro CA
Flavocytochrome c3 from Shewanella frigidimarina (fcc3) is a tetrahaem periplasmic protein of 64 kDa with fumarate reductase activity. This work reports the first example of NMR...
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[NMR paper] Structure of recombinant human parathyroid hormone in solution using multidimensional
Structure of recombinant human parathyroid hormone in solution using multidimensional NMR spectroscopy.
Related Articles Structure of recombinant human parathyroid hormone in solution using multidimensional NMR spectroscopy.
Biol Chem Hoppe Seyler. 1996 Mar;377(3):175-86
Authors: Gronwald W, Schomburg D, Harder MP, Mayer H, Paulsen J, Wingender E, Wray V
The solution structure of human parathyroid hormone, in the form of recombinant prolyl-hPTH(1-84), has been investigated by multidimensional NMR spectroscopy under conditions (aqueous...
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[NMR paper] Conformation of parathyroid hormone antagonists by CD, NMR, and molecular dynamics si
Conformation of parathyroid hormone antagonists by CD, NMR, and molecular dynamics simulations.
Related Articles Conformation of parathyroid hormone antagonists by CD, NMR, and molecular dynamics simulations.
Biopolymers. 1995 Oct;36(4):485-95
Authors: Chorev M, Behar V, Yang Q, Rosenblatt M, Mammi S, Maretto S, Pellegrini M, Peggion E
The conformation of two highly potent parathyroid hormone (PTH) antagonists was investigated in water/2,2,2-trifluoroethanol mixtures. The two peptides are derived from the sequence (7-34) of PTH and of...
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[NMR paper] Studies on the three-dimensional behaviour of the selectin ligands Lewis(a) and sulph
Studies on the three-dimensional behaviour of the selectin ligands Lewis(a) and sulphated Lewis(a) using NMR spectroscopy and molecular dynamics simulations.
Related Articles Studies on the three-dimensional behaviour of the selectin ligands Lewis(a) and sulphated Lewis(a) using NMR spectroscopy and molecular dynamics simulations.
Glycobiology. 1994 Feb;4(1):49-57
Authors: Kogelberg H, Rutherford TJ
Sulphated blood group Lewis(a)/Lewis(x) (Le(a)/Le(x)) type sequences, with sulphate at the 3-position of galactose, have emerged as potent ligands...
[NMR paper] Studies on the three-dimensional behaviour of the selectin ligands Lewis(a) and sulph
Studies on the three-dimensional behaviour of the selectin ligands Lewis(a) and sulphated Lewis(a) using NMR spectroscopy and molecular dynamics simulations.
Related Articles Studies on the three-dimensional behaviour of the selectin ligands Lewis(a) and sulphated Lewis(a) using NMR spectroscopy and molecular dynamics simulations.
Glycobiology. 1994 Feb;4(1):49-57
Authors: Kogelberg H, Rutherford TJ
Sulphated blood group Lewis(a)/Lewis(x) (Le(a)/Le(x)) type sequences, with sulphate at the 3-position of galactose, have emerged as potent ligands...
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[NMR paper] Stabilized NMR structure of human parathyroid hormone(1-34).
Stabilized NMR structure of human parathyroid hormone(1-34).
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 Stabilized NMR structure of human parathyroid hormone(1-34).
Eur J Biochem. 1993 Jul 15;215(2):315-21
Authors: Barden JA, Cuthbertson RM
The structure of the biologically-active N-terminal region of human parathyroid hormone, PTH(1-34), was investigated in the presence of 10% trifluoroethanol using two-dimensional proton...