Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins.

[1]  C. Tanford Contribution of Hydrophobic Interactions to the Stability of the Globular Conformation of Proteins , 1962 .

[2]  J. C. Kendrew,et al.  Structure and function of haemoglobin: II. Some relations between polypeptide chain configuration and amino acid sequence , 1965 .

[3]  M. Schiffer,et al.  Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. , 1967, Biophysical journal.

[4]  P Dunnill,et al.  The use of helical net-diagrams to represent protein structures. , 1968, Biophysical journal.

[5]  J. M. Zimmerman,et al.  The characterization of amino acid sequences in proteins by statistical methods. , 1968, Journal of theoretical biology.

[6]  B. Lee,et al.  The interpretation of protein structures: estimation of static accessibility. , 1971, Journal of molecular biology.

[7]  Irwin D. Kuntz,et al.  Hydration of macromolecules. III. Hydration of polypeptides , 1971 .

[8]  Akintola A. Aboderin,et al.  An empirical hydrophobicity scale for α-amino-acids and some of its applications , 1971 .

[9]  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.

[10]  A. Shrake,et al.  Environment and exposure to solvent of protein atoms. Lysozyme and insulin. , 1973, Journal of molecular biology.

[11]  H. Bull,et al.  Surface tension of amino acid solutions: a hydrophobicity scale of the amino acid residues. , 1974, Archives of biochemistry and biophysics.

[12]  C. Chothia,et al.  Hydrophobic bonding and accessible surface area in proteins , 1974, Nature.

[13]  V. Lim Algorithms for prediction of α-helical and β-structural regions in globular proteins , 1974 .

[14]  V. Lim Structural principles of the globular organization of protein chains. A stereochemical theory of globular protein secondary structure. , 1974, Journal of molecular biology.

[15]  D. D. Jones,et al.  Amino acid properties and side-chain orientation in proteins: a cross correlation appraoch. , 1975, Journal of theoretical biology.

[16]  C. Chothia Structural invariants in protein folding , 1975, Nature.

[17]  M. Levitt A simplified representation of protein conformations for rapid simulation of protein folding. , 1976, Journal of molecular biology.

[18]  C. Chothia The nature of the accessible and buried surfaces in proteins. , 1976, Journal of molecular biology.

[19]  H. Scheraga,et al.  Medium- and long-range interaction parameters between amino acids for predicting three-dimensional structures of proteins. , 1976, Macromolecules.

[20]  A. Mclachlan,et al.  The 14-fold periodicity in α-tropomyosin and the interaction with actin , 1976 .

[21]  George D. Rose,et al.  Prediction of chain turns in globular proteins on a hydrophobic basis , 1978, Nature.

[22]  H A Scheraga,et al.  Influence of water on protein structure. An analysis of the preferences of amino acid residues for the inside or outside and for specific conformations in a protein molecule. , 1978, Macromolecules.

[23]  J. Janin,et al.  Surface and inside volumes in globular proteins , 1979, Nature.

[24]  A. Komoriya,et al.  Local interactions as a structure determinant for protein molecules: III. , 1979, Biochimica et biophysica acta.

[25]  Gunnar von Heijne,et al.  Trans‐membrane Translocation of Proteins , 1979 .

[26]  D J Osguthorpe,et al.  Refined models for computer simulation of protein folding. Applications to the study of conserved secondary structure and flexible hinge points during the folding of pancreatic trypsin inhibitor. , 1979, Journal of molecular biology.

[27]  P. Ponnuswamy,et al.  Spatial assignment of amino acid residues in globular proteins: an approach from information theory. , 1980, Journal of theoretical biology.

[28]  K Nishikawa,et al.  Prediction of the surface-interior diagram of globular proteins by an empirical method. , 2009, International journal of peptide and protein research.

[29]  K. Olsen,et al.  Internal residue criteria for predicting three-dimensional protein structures. , 1980, Biochimica et biophysica acta.

[30]  P. Ponnuswamy,et al.  Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins. , 1980, Biochimica et biophysica acta.

[31]  S. Rackovsky,et al.  Empirical Studies of Hydrophobicity. 1. Effect of Protein Size on the Hydrophobic Behavior of Amino Acids , 1980 .

[32]  P M Cullis,et al.  Affinities of amino acid side chains for solvent water. , 1981, Biochemistry.

[33]  R. Cramer,et al.  Measurement of correlation of partition coefficients of polar amino acids. , 1981, Molecular pharmacology.

[34]  R. Doolittle,et al.  A simple method for displaying the hydropathic character of a protein. , 1982, Journal of molecular biology.

[35]  B. Zaslavsky,et al.  Measurement of relative hydrophobicity of amino acid side-chains by partition in an aqueous two-phase polymeric system: Hydrophobicity scale for non-polar and ionogenic side-chains , 1982 .

[36]  M. Charton,et al.  The structural dependence of amino acid hydrophobicity parameters. , 1982, Journal of theoretical biology.

[37]  David Eisenberg,et al.  The helical hydrophobic moment: a measure of the amphiphilicity of a helix , 1982, Nature.

[38]  W. Kabsch,et al.  Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.

[39]  D. Eisenberg,et al.  Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure. , 1983, Journal of molecular biology.

[40]  C. Frömmel,et al.  The apolar surface area of amino acids and its empirical correlation with hydrophobic free energy. , 1984, Journal of theoretical biology.

[41]  G. Rose,et al.  Hydrophobicity of amino acid residues in globular proteins. , 1985, Science.

[42]  R. Jernigan,et al.  Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation , 1985 .

[43]  G. Rose,et al.  Turns in peptides and proteins. , 1985, Advances in protein chemistry.

[44]  H. Guy Amino acid side-chain partition energies and distribution of residues in soluble proteins. , 1985, Biophysical journal.

[45]  C. DeLisi,et al.  Prediction of protein structural class from the amino acid sequence , 1986, Biopolymers.

[46]  A. D. McLachlan,et al.  Solvation energy in protein folding and binding , 1986, Nature.

[47]  T. Hopp,et al.  Protein surface analysis. Methods for identifying antigenic determinants and other interaction sites. , 1986, Journal of immunological methods.

[48]  J L Cornette,et al.  Prediction of immunodominant helper T cell antigenic sites from the primary sequence. , 1987, Journal of immunology.