Related ArticlesThe NMR structure of human obestatin in membrane-like environments: insights into the structure-bioactivity relationship of obestatin.
PLoS One. 2012;7(10):e45434
Authors: Alén BO, Nieto L, Gurriarán-Rodríguez U, Mosteiro CS, Álvarez-Pérez JC, Otero-Alén M, Camiña JP, Gallego R, García-Caballero T, Martín-Pastor M, Casanueva FF, Jiménez-Barbero J, Pazos Y
Abstract
The quest for therapeutic applications of obestatin involves, as a first step, the determination of its 3D solution structure and the relationship between this structure and the biological activity of obestatin. On this basis, we have employed a combination of circular dichroism (CD), nuclear magnetic resonance (NMR) spectroscopy, and modeling techniques to determine the solution structure of human obestatin (1). Other analogues, including human non-amidated obestatin (2) and the fragment peptides (6-23)-obestatin (3), (11-23)-obestatin (4), and (16-23)-obestatin (5) have also been scrutinized. These studies have been performed in a micellar environment to mimic the cell membrane (sodium dodecyl sulfate, SDS). Furthermore, structural-activity relationship studies have been performed by assessing the in vitro proliferative capabilities of these peptides in the human retinal pigmented epithelial cell line ARPE-19 (ERK1/2 and Akt phosphorylation, Ki67 expression, and cellular proliferation). Our findings emphasize the importance of both the primary structure (composition and size) and particular segments of the obestatin molecule that posses significant ?-helical characteristics. Additionally, details of a species-specific role for obestatin have also been hypothesized by comparing human and mouse obestatins (1 and 6, respectively) at both the structural and bioactivity levels.
[NMR paper] Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Related Articles Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Annu Rev Biophys. 2013 Mar 22;
Authors: Comellas G, Rienstra CM
Abstract
Protein structure determination methods using magic-angle spinning solidstate nuclear magnetic resonance (MAS SSNMR) have experienced a remarkable...
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[NMR paper] NMR structure note: the structure of human calcium-bound S100A11.
NMR structure note: the structure of human calcium-bound S100A11.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR structure note: the structure of human calcium-bound S100A11.
J Biomol NMR. 2012 Oct;54(2):211-5
Authors: Hung KW, Chang YM, Yu C
PMID: 22903637
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NMR structure note: the structure of human calcium-bound S100A11
NMR structure note: the structure of human calcium-bound S100A11
NMR structure note: the structure of human calcium-bound S100A11
Content Type Journal Article
Category NMR structure note
Pages 1-5
DOI 10.1007/s10858-012-9661-2
Authors
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Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.
Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.
Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.
Biochim Biophys Acta. 2011 Jul 23;
Authors: Cohen LS, Arshava B, Neumoin A, Becker JM, Güntert P, Zerbe O, Naider F
Fragments of integral membrane proteins have been used to study the physical chemical properties of regions of transporters and receptors. Ste2p(G31-T110) is an 80-residue polypeptide which contains a...
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07-28-2011 10:51 AM
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
Eur Biophys J. 2011 Apr;40(4):447-62
Authors: Toke O, Bánóczi Z, Király P, Heinzmann R, Bürck J, Ulrich AS, Hudecz F
Maximin-4 is a 27-residue cationic antimicrobial peptide exhibiting selectivity for bacterial cells. As part of the innate defense system in the Chinese red-belly...
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07-20-2011 10:00 AM
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Protein Sci. 2011 Feb 22;
Authors: Hong M, Su Y
Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier to insert into the...
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02-24-2011 11:04 AM
[NMR paper] 1H-NMR assignments and local environments of aromatic residues in bovine, human and g
1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin.
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 1H-NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of alpha-lactalbumin.
Eur J Biochem. 1992 Dec 15;210(3):699-709
Authors: Alexandrescu AT, Broadhurst RW, Wormald C, Chyan CL, Baum J, Dobson CM
1H-NMR...
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[NMR paper] Relationship between electrostatics and redox function in human thioredoxin: characte
Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR.
Related Articles Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR.
Biochemistry. 1992 Apr 7;31(13):3442-52
Authors: Forman-Kay JD, Clore GM, Gronenborn AM
The electrostatic behavior of potentially titrating groups in reduced human thioredoxin was investigated...
The NMR structure of human obestatin in membrane-like environments: insights into the structure-bioactivity relationship of obestatin.
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