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Hicks, June H.

doi:10.1111/j.1944-9720.2001.tb02116.x

Cited by 6 publications

(10 citation statements)

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“…This assumption is based on the work of Opella and co-workers 35 who reported using one-dimensional (1D) and 2D solid-state 15 N NMR methods that magainin 2 adopts a ␣-helical conformation that is oriented parallel to the surface of the lipid bilayers. Solution state NMR studies cannot be used to determine the orientation of a peptide relative to the surface of a micelle.…”

Section: Molecular Modelingmentioning

confidence: 99%

Comparison of the conformation and electrostatic surface properties of magainin peptides bound to sodium dodecyl sulfate and dodecylphosphocholine micelles

et al. 2003

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The role played by noncovalent interactions in inducing a stable secondary structure onto the sodium dodecyl sulfate (SDS) and dodecylphosphocholine (DPC) micelle-bound conformations of (Ala(8,13,18))magainin 2 amide and the DPC micelle bound conformation of magainin 1 were determined. Two-dimensional NMR and molecular modeling investigations indicated that (Ala(8,13,18))magainin 2 amide bound to DPC micelles adopts a alpha-helical secondary structure involving residues 2-16. The four C-terminal residues converge to a lose beta-turn structure. (Ala(8,13,18))magainin 2 amide bound to SDS miscelles adopts a alpha-helical secondary structure involving residues 7-18. The C- and N-terminal residues exhibited a great deal of conformational flexibility. Magainin 1 bound to DPC micelles adopts a alpha-helical secondary structure involving residues 4-19. The C-terminal residues converge to a lose beta-turn structure. The results of this investigation indicate hydrophobic interactions are the major contributors to stabilizing the induced helical structure of the micelle-bound peptides. Electrostatic interactions between the polar head groups of the micelle and the cationic side chains of the peptides define the positions along the peptide backbone where the helical structures begin and end.

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Section: Molecular Modelingmentioning

confidence: 99%

Comparison of the conformation and electrostatic surface properties of magainin peptides bound to sodium dodecyl sulfate and dodecylphosphocholine micelles

et al. 2003

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“…9À11 Despite the tremendous interest in this molecule, only a fraction of its structure is characterized in detail. Circular dichroism, 12 Raman spectroscopy, 13 nuclear magnetic resonance, 14 and molecular modeling studies reveal that the BK Ser 6 ÀPro 7 ÀPhe 8 ÀArg 9 residues favor a β-turn motif, 15 whereas the region Arg 1 ÀPhe 5 is apparently unstructured. This combination of ordered and disordered regions hinders a complete determination of the BK structure.…”

mentioning

confidence: 99%

“…The solution-phase simulations appear to capture the Ser 6 ÀArg 9 β-turn motif (in three of the four structural types), consistent with experimental measurements in solution. 14, 15 The Arg 1 ÀPhe 5 region shows structural variations that arise from charge solvation of the guanidine group of Arg 1 by backbone carbonyl groups. Other populations (not shown) have cross sections that match the E and F peaks.…”

mentioning

confidence: 99%

Number of Solution States of Bradykinin from Ion Mobility and Mass Spectrometry Measurements

et al. 2011

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Ion mobility and mass spectrometry measurements have been used to examine the populations of different solution structures of the nonapeptide bradykinin. Over the range of solution compositions studied, from 0:100 to 100:0 methanol:water and 0:100 to 90:10 dioxane:water, evidence for ten independent populations of bradykinin structures in solution is found. In some solutions as many as eight structures may coexist. The solution populations are substantially different than the gas-phase equilibrium distribution of ions, which exhibits only three distinct states. Such a large number of coexisting structures explains the inability of traditional methods of characterization such as nuclear magnetic resonance spectroscopy and crystallography to determine detailed structural features for some regions of this peptide.

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“…An extensive review of the role of NMR in rational drug design was published by Hicks. 44 This review begins with the contributions pulsed field gradients have made to the facile measurement of diffusion coefficients. It then delves into the logic of the SAR by NMR method developed by Fesik and the NOE pumping techniques devised by Shapiro.…”

Section: Nmr Methods Used In Combinatorial Chemistry/sar By Nmrmentioning

confidence: 99%