Brasseur, R. 1991. Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations. J. Biol. Chem. 266: 16120-16127.
Chothia, C. 1976. The nature of the accessible and buried surfaces in proteins. J. Mol. Biol. 105: 1-12.
Chou, K.C., Zhang, C.T., and Maggiora, G.M. 1997. Disposition of amphiphilic helices in heteropolar environments. Proteins 28: 99-108.
Creighton, T. 1993. Chemical properties of polypeptides. In Chemical properties of polypeptides (ed. T. Creighton), pp. 1-46. W.H. Freeman and Company, New York.
Eisenhaber, F. and Argos, P. 1996. Hydrophobic regions on protein surfaces: Definition based on hydration shell structure and a quick method for their computation. Protein Eng. 9: 1121-1133.
Flower, D.R. 1997. SERF: A program for accessible surface area calculations. J. Mol. Graph. Model. 15: 238-244.
Jones, S. and Thornton, J.M. 1997. Analysis of protein-protein interaction sites using surface patches. J. Mol. Biol. 272: 121-132.
Li, L., Darden, T.A., Bartolotti, L., Kominos, D., and Pedersen, L.G. 1999. An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments. Biophys. J. 76: 2871-2878.
Li, X. and Pan, X.M. 2001. New method for accurate prediction of solvent accessibility from protein sequence. Proteins 42: 1-5.
Liu, W. and Chou, K.C. 1999. Prediction of protein secondary structure content. Protein Eng. 12: 1041-1050.
Naderi-Manesh, H., Sadeghi, M., Arab, S., and Moosavi Movahedi, A.A. 2001. Prediction of protein surface accessibility with information theory. Proteins 42: 452-459.
Rost, B. 1996. PHD: Predicting one-dimensional protein structure by profilebased neural networks. Methods Enzymol. 266: 525-539.
Rost, B. and Sander, C. 1994. Conservation and prediction of solvent accessibility in protein families. Proteins 20: 216-226.
Samanta, U., Bahadur, R.P., and Chakrabarti, P. 2002. Quantifying the accessible surface area of protein residues in their local environment. Protein Eng. 15: 659-667.
Schladitz, C., Vieira, E.P., Hermel, H., and Mohwald, H. 1999. Amyloid-β-sheet formation at the air-water interface. Biophys. J. 77: 3305-3310.
Shrake, A. and Rupley, J.A. 1973. Environment and exposure to solvent of protein atoms. Lysozyme and insulin. J. Mol. Biol. 79: 351-371.
Srinivasan, R. and Rose, G.D. 1995. LINUS: A hierarchic procedure to predict the fold of a protein. Proteins 22: 81-99.
Tanford, C. 1973. In The hydrophobic effect: Formation of micelles and biological membranes (ed. C. Tanford). pp. 5-20, Wiley, New York.
Thomas, A., Bouffioux, O., Geeurickx, D., and Brasseur, R. 2001. Pex, analytical tools for PDB files. I. GF-Pex: Basic file to describe a protein. Proteins 43: 28-36.
Thomas, A., Meurisse, R., Charloteaux, B., and Brasseur, R. 2002a. Aromatic side-chain interactions in proteins. I. Main structural features. Proteins 48: 628-634.
Thomas, A., Meurisse, R., and Brasseur, R. 2002b. Aromatic side-chain interactions in proteins. II. Near- and far-sequence Phe-X pairs. Proteins 48: 635-644.
Yuan, Z., Burrage, K., and Mattick, J.S. 2002. Prediction of protein solvent accessibility using support vector machines. Proteins 48: 566-570.
