scholarly article | Q13442814 |
P2093 | author name string | Goodfellow JM | |
Bodkin MJ | |||
P2860 | cites work | Structural basis of amino acid alpha helix propensity | Q27732169 |
Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins | Q28240446 | ||
Amino acid preferences for specific locations at the ends of alpha helices | Q29618508 | ||
Alpha-helix stabilization by natural and unnatural amino acids with alkyl side chains | Q30390051 | ||
Helix signals in proteins | Q30400745 | ||
The helical s constant for alanine in water derived from template-nucleated helices | Q31162195 | ||
Straight-chain non-polar amino acids are good helix-formers in water. | Q34109377 | ||
Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design | Q34376818 | ||
The mechanism of alpha-helix formation by peptides | Q35836992 | ||
Stabilization of alpha-helical structures in short peptides via end capping | Q36077158 | ||
A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A | Q36291131 | ||
Helix capping propensities in peptides parallel those in proteins | Q36701813 | ||
Weakly polar interactions in proteins. | Q39573010 | ||
Design of peptides and proteins | Q39573016 | ||
Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an alpha-helical region of carboxypeptidase A. | Q41161629 | ||
Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings | Q41811876 | ||
A single carboxy-terminal arginine determines the amino-terminal helix conformation of an alanine-based peptide | Q43022332 | ||
Effect of alanine versus glycine in alpha-helices on protein stability | Q43795904 | ||
Molecular dynamics simulations of the unfolding of an alpha-helical analogue of ribonuclease A S-peptide in water | Q44354473 | ||
Perturbation of peptide conformations induced in anisotropic environments | Q44623367 | ||
Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance | Q44634743 | ||
Unfolding of an ?-helix in water | Q44974805 | ||
Relative helix-forming tendencies of nonpolar amino acids | Q46587484 | ||
Large differences in the helix propensities of alanine and glycine | Q46971709 | ||
Cutoff size does strongly influence molecular dynamics results on solvated polypeptides | Q47410616 | ||
Molecular dynamics simulations of helix denaturation | Q47637533 | ||
Elucidating the folding problem of helical peptides using empirical parameters. | Q52376869 | ||
Residue helix parameters obtained from dichroic analysis of peptides of defined sequence. | Q52393344 | ||
Tests of the helix dipole model for stabilization of α-helices | Q59076470 | ||
Position effect on apparent helical propensities in the C-peptide helix | Q68045156 | ||
Analysis of the relationship between side-chain conformation and secondary structure in globular proteins | Q68541264 | ||
Effect of central-residue replacements on the helical stability of a monomeric peptide | Q68577440 | ||
Water-inserted alpha-helical segments implicate reverse turns as folding intermediates | Q69633330 | ||
The (i, i + 4) Phe-His interaction studied in an alanine-based alpha-helix | Q70602565 | ||
Helix-coil transition of the isolated amino terminus of ribonuclease | Q71758379 | ||
The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale | Q71785195 | ||
A measure of helical propensity for amino acids in membrane environments | Q72033170 | ||
Hydrogen bond strength and beta-sheet propensities: the role of a side chain blocking effect | Q72511006 | ||
Design of helix ends. Amino acid preferences, hydrogen bonding and electrostatic interactions | Q72802590 | ||
P433 | issue | 4 | |
P304 | page(s) | 603-612 | |
P577 | publication date | 1995-04-01 | |
P1433 | published in | Protein Science | Q7251445 |
P1476 | title | Competing interactions contributing to alpha-helical stability in aqueous solution | |
P478 | volume | 4 |
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