Molecular dynamics simulation of the stability of a 22‐residue α‐helix in water and 30% trifluoroethanol
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[1] M. Räsänen,et al. Ab initio calculations on ethanol and 2-substituted fluorine and chlorine containing mono-, di- and tri-haloethanols, with reference to conformer interconversions at low temperatures , 1984 .
[2] G. Borin,et al. The influence of amino acid side-chains on alpha-helix stability: S-peptide analogues and related ribonucleases S'. , 1976, Journal of molecular biology.
[4] I. Kuntz,et al. A molecular dynamics simulation of polyalanine: An analysis of equilibrium motions and helix–coil transitions , 1991, Biopolymers.
[5] S. Ishiguro,et al. Intramolecular and liquid structure of 2,2,2-trifluoroethanol by X-ray diffraction , 1989 .
[6] I D Kuntz,et al. Molecular dynamics simulations of small peptides: Dependence on dielectric model and pH , 1991, Biopolymers.
[7] L. Gierasch,et al. Side chain–backbone hydrogen bonding contributes to helix stability in peptides derived from an α‐helical region of carboxypeptidase A , 1991, Proteins.
[8] H. Berendsen,et al. Molecular dynamics with coupling to an external bath , 1984 .
[9] P. Gooley,et al. Location of an alpha-helix in fragment 96-133 from bovine somatotropin by 1H NMR spectroscopy. , 1988, Biochemistry.
[10] G. Borin,et al. Conformational properties of the N‐terminal residues of S‐peptide. II. The guanidine hydrochloride–water–trifluoroethanol system , 1978 .
[11] C. Tanford,et al. The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. , 1971, The Journal of biological chemistry.
[12] J. V. van Noort,et al. Catheptic processing of protein antigens: enzymic and molecular aspects. , 1990, Seminars in immunology.
[13] J Tirado-Rives,et al. Molecular dynamics simulations of the unfolding of an alpha-helical analogue of ribonuclease A S-peptide in water. , 1991, Biochemistry.
[14] Lennart Nilsson,et al. Molecular dynamics simulation of galanin in aqueous and nonaqueous solution , 1992 .
[15] P E Wright,et al. Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix. , 1988, Journal of molecular biology.
[16] F. Bermejo,et al. Thermodynamic parameters for the helix–coil thermal transition of ribonuclease‐S‐peptide and derivatives from 1H‐nmr data , 1986, Biopolymers.
[17] N. Kallenbach,et al. Stabilization of the ribonuclease S‐peptide α‐helix by trifluoroethanol , 1986 .
[18] P. Y. Chou,et al. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. , 1974, Biochemistry.
[19] M. Llinás,et al. Solution conformation of the ferrichromes. VI. Charge relay at the peptide bond. Proton magnetic resonance study of solvation effects on the amide electron density distribution , 1975 .
[20] M Levitt,et al. Molecular dynamics simulations of helix denaturation. , 1992, Journal of molecular biology.
[21] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[22] H. Berendsen,et al. ALGORITHMS FOR MACROMOLECULAR DYNAMICS AND CONSTRAINT DYNAMICS , 1977 .
[23] L. Moroder,et al. Studies on cytochrome c. XI. Circular dichroism studies on synthetic peptides related to the C‐terminal region of baker's yeast iso‐1‐cytochrome c , 1975 .
[24] B. Zimm,et al. Theory of the Phase Transition between Helix and Random Coil in Polypeptide Chains , 1959 .