[NMR paper] Micelle-bound conformations of neurohypophyseal hormone analogues modified with a C?-disubstituted residue: NMR and molecular modelling studies.
Related ArticlesMicelle-bound conformations of neurohypophyseal hormone analogues modified with a C?-disubstituted residue: NMR and molecular modelling studies.
J Biomol Struct Dyn. 2013;31(7):748-64
Authors: Sikorska E, Kwiatkowska A
Abstract
In this study, by applying a combined approach of NMR measurements and molecular modelling, the conformations and the interactions with membrane-like environment of five arginine vasopressin (AVP) or oxytocin (OT) analogues modified with C?-disubstituted cis-1-amino-4-phenylcyclohexane-1-carboxylic acid in position 2 have been determined. In addition, the AVP analogues were prepared in N-acylated forms with various bulky acyl groups. All of the peptides studied interacted with the mixed dodecylphosphocholine:sodium dodecyl sulphate micelle, providing a model of biological membrane. A different polarities of the AVP- and OT-like peptides resulted in their different position relative to the micelle surface. Thus, the arrangement of the former was nearly perpendicular, whereas the latter was rather parallel to the micelle's surface. Moreover, the results of our studies have shown that the binding sites for antagonists may be overlapped with that for agonists, as well as it may be quite different. Nevertheless, the aromatic-aromatic contacts represent the most important interactions for antagonists, whereas the hydrophilic interactions seem to be crucial for agonists.
[NMR paper] Synthesis, 2D-NMR and molecular modelling studies of pentacycloundecane lactam-peptides and peptoids as potential HIV-1 wild type C-SA protease inhibitors.
Synthesis, 2D-NMR and molecular modelling studies of pentacycloundecane lactam-peptides and peptoids as potential HIV-1 wild type C-SA protease inhibitors.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--informahealthcare.com-userimages-ContentEditor-1258375244362-ihc-linkout.gif Related Articles Synthesis, 2D-NMR and molecular modelling studies of pentacycloundecane lactam-peptides and peptoids as potential HIV-1 wild type C-SA protease inhibitors.
J Enzyme Inhib Med Chem. 2013 Feb;28(1):78-88
Authors: Makatini MM, Petzold K, Alves...
[NMR paper] NMR conformational studies of micelle-bound orexin-B: a neuropeptide involved in the
NMR conformational studies of micelle-bound orexin-B: a neuropeptide involved in the sleep/awake cycle and feeding regulation.
Related Articles NMR conformational studies of micelle-bound orexin-B: a neuropeptide involved in the sleep/awake cycle and feeding regulation.
J Biomol Struct Dyn. 2003 Dec;21(3):341-51
Authors: Miskolzie M, Lucyk S, Kotovych G
The preferred conformation of orexin-B, an orphan G-protein coupled receptor agonist (the human sequence is RSGPPGLQGRLQRLLQASGNHAAGILTM-NH(2)) has been determined by (1)H and (13)C 2D NMR...
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[NMR paper] Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular d
Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular dynamics study.
Related Articles Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular dynamics study.
Biopolymers. 2002 Nov 15;65(4):284-98
Authors: Dixon AM, Venable RM, Pastor RW, Bull TE
A peptide fragment from a protein hairpin turn region was modified by addition of isoleucine residues to both ends to enhance binding to lipid micelles; the resulting peptide (I(1)-I(2)-C(3)-N(4)-N(5)-P(6)-H(7)-I(8)-I(9)) contains the core...
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[NMR paper] 1H and 13C NMR assignments and molecular modelling of a minor groove DNA-binding pept
1H and 13C NMR assignments and molecular modelling of a minor groove DNA-binding peptide from the HMG-I protein.
Related Articles 1H and 13C NMR assignments and molecular modelling of a minor groove DNA-binding peptide from the HMG-I protein.
Int J Pept Protein Res. 1995 Jun;45(6):554-60
Authors: Evans JN, Zajicek J, Nissen MS, Munske G, Smith V, Reeves R
The HMG-I subfamily of high mobility group (HMG) chromatin proteins consists of DNA-binding proteins that preferentially bind to stretches of A.T-rich sequence both in vitro and in vivo....
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08-22-2010 03:41 AM
[NMR paper] NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein
NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein.
J Neurochem. 1994 Jan;62(1):349-54
Authors: Klunk WE, Xu CJ, Pettegrew JW
The beta/A4-amyloid protein (beta/A4) and many synthetic fragments of this protein have proved to be very difficult to solubilize, leading to...
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[NMR paper] NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein
NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein.
J Neurochem. 1994 Jan;62(1):349-54
Authors: Klunk WE, Xu CJ, Pettegrew JW
The beta/A4-amyloid protein (beta/A4) and many synthetic fragments of this protein have proved to be very difficult to solubilize, leading to...
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08-22-2010 03:33 AM
[NMR paper] 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle.
2D NMR and structural model for a mitochondrial signal peptide bound to a micelle.
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Biochemistry. 1990 Oct 23;29(42):9872-8
Authors: Karslake C, Piotto ME, Pak YK, Weiner H, Gorenstein DG
The 19 amino acid signal peptide of rat liver aldehyde dehydrogenase, possessing a lysine substitution for an arginine and containing 3 extra amino acid residues at the C terminus, was studied by two-dimensional NMR in a dodecylphosphocholine micelle. In this...
Micelle-bound conformations of neurohypophyseal hormone analogues modified with a C?-disubstituted residue: NMR and molecular modelling studies.
Linear Mode
