Related ArticlesConformation propensities of des-acyl-ghrelin as probed by CD and NMR.
Peptides. 2013 May;43:62-7
Authors: De Ricco R, Valensin D, Gaggelli E, Valensin G
Abstract
Des-acyl-ghrelin is a 28 amino acid peptide secreted by both human and rat stomach. Together with ghrelin and obestatin, it is obtained by post-translational modification of a 117 aminoacid prepropeptide mainly expressed in distinct endocrine cell type in the stomach. Although its receptor has not been unambiguously identified so far, des-acyl-ghrelin is considered one of the strongest antagonists of ghrelin in activating the growth hormone secretagogue receptor (GHS-R). Here the secondary structure of des-acyl-ghrelin in different experimental conditions has been investigated and compared with that of obestatin, a bioactive peptide having similar biological functions. CD and NMR techniques have been combined for gaining the desired conformational features. The obtained structures support a steady alpha-helix structure spanning residues from 7 to 14, very similar to that observed for obestatin at the same experimental conditions, leading to suggest that a similar secondary structure can be associated with the similar biological role.
[NMR paper] Modified sham feeding of foods with different macronutrient compositions differentially influences cephalic change of insulin, ghrelin and NMR-based metabolomic profiles.
Modified sham feeding of foods with different macronutrient compositions differentially influences cephalic change of insulin, ghrelin and NMR-based metabolomic profiles.
Related Articles Modified sham feeding of foods with different macronutrient compositions differentially influences cephalic change of insulin, ghrelin and NMR-based metabolomic profiles.
Physiol Behav. 2014 Jun 18;
Authors: Zhu Y, Hsu WH, Hollis JH
Abstract
Little is known about the effect of macronutrient composition of foods on cephalic phase response of...
nmrlearner
Journal club
0
06-22-2014 12:24 PM
[NMR paper] Conformational Propensities of Intrinsically Disordered Proteins from NMR Chemical Shifts.
Conformational Propensities of Intrinsically Disordered Proteins from NMR Chemical Shifts.
Related Articles Conformational Propensities of Intrinsically Disordered Proteins from NMR Chemical Shifts.
Chemphyschem. 2013 Jun 21;
Authors: Kragelj J, Ozenne V, Blackledge M, Jensen MR
Abstract
The realization that a protein can be fully functional even in the absence of a stable three-dimensional structure has motivated a large number of studies describing the conformational behaviour of these proteins at atomic resolution. Here, we review...
nmrlearner
Journal club
0
06-26-2013 09:39 AM
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt 9):1137-40
Authors: Barnwal RP, Van Voorhis WC, Varani G
Abstract
Nearly complete resonance assignment and the high-resolution NMR structure of the acyl-carrier protein from Borrelia burgdorferi, a target of the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure-determination pipeline, are reported. This protein...
nmrlearner
Journal club
0
09-10-2011 06:51 PM
[NMR paper] Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase reveal
Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase revealed by NMR spectroscopy.
Related Articles Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase revealed by NMR spectroscopy.
J Am Chem Soc. 2005 Jun 15;127(23):8424-32
Authors: Wu J, Bell AF, Jaye AA, Tonge PJ
Medium-chain acyl-CoA dehydrogenase (MCAD) catalyzes the flavin-dependent oxidation of fatty acyl-CoAs to the corresponding trans-2-enoyl-CoAs. The interaction of hexadienoyl-CoA (HD-CoA), a product analogue, with recombinant pig...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[NMR paper] Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues
Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a beta-hairpin peptide.
Related Articles Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a beta-hairpin peptide.
J Mol Biol. 1998 Dec 18;284(5):1597-609
Authors: Griffiths-Jones SR, Sharman GJ, Maynard AJ, Searle MS
Analysis of residues in coil regions of protein structures...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] C-NMR study on the interaction of medium-chain acyl-CoA dehydrogenase with acetoacety
C-NMR study on the interaction of medium-chain acyl-CoA dehydrogenase with acetoacetyl-CoA.
Related Articles C-NMR study on the interaction of medium-chain acyl-CoA dehydrogenase with acetoacetyl-CoA.
J Biochem. 1996 Mar;119(3):512-9
Authors: Miura R, Nishina Y, Fuji S, Shiga K
The change-transfer interaction in the complex of pig kidney medium-chain acyl-CoA dehydrogenase (MCAD) with acetoacetyl-CoA was investigated by 13C-NMR spectroscopy and molecular orbital treatment. The acyl carbons of acetoacetyl-CoA were separately 13C-labeled and...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver:
The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy.
Related Articles The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy.
J Biomol NMR. 1993 May;3(3):271-84
Authors: Andersen KV, Poulsen FM
The 3D structure of bovine recombinant acyl-coenzyme A binding protein has been determined using multidimensional heteronuclear magnetic...
nmrlearner
Journal club
0
08-21-2010 11:53 PM
[NMR paper] Refinement of the NMR structures for acyl carrier protein with scalar coupling data.
Refinement of the NMR structures for acyl carrier protein with scalar coupling data.
Related Articles Refinement of the NMR structures for acyl carrier protein with scalar coupling data.
Proteins. 1990;8(4):377-85
Authors: Kim Y, Prestegard JH
Structure determination of small proteins using NMR data is most commonly pursued by combining NOE derived distance constraints with inherent constraints based on chemical bonding. Ideally, one would make use of a variety of experimental observations, not just distance constraints. Here, coupling...
Conformation propensities of des-acyl-ghrelin as probed by CD and NMR.
Linear Mode
