Qian, N. and Sejnowski, T. J. (1988). Predicting the secondary structure of globular proteins using neural network models. J. Mol. Biol. 202; 865-884

Rafalski, J. A. (1986). Structure of wheat gamma-gliadin genes. Gene 43; 221-229.

Ramachandran, G. N., Ramakrishnan, C. and Sasisekharan, V. (1963). Stereochemistry of Polypeptide Chain Configurations. J. Mol. Biol. 7; 95-99

Rao, S. T. and Rossmann, M. G. (1973). Comparison of super-secondary structures in proteins. J. Mol. Biol. 76; 241-256.

Rebek, J., Jr., Marshall, L., Wolak, R., Parris, K., Killoran, M., Askew, B., Nemeth, D. and Islam, N. (1985). Convergent functional groups: Synthetic and structural studies. J. Am. Chem. Soc. 107; 7476-7481.

Rebek, J., Jr., Duff, R. J., Gordon, W.E., and Parris, K., (1986). Convergent functional groups provide a measure of stereoelectronic effects at carbonyl oxygen. J. Am. Chem. Soc. 108; 6068-6069.

Reddy, I. M., Kella, N. D. K. and Kinsella, J. E. (1988). Structural and Conformational Basis of the Resistance of beta-lactoglobulin to Peptic and Chymotryptic Digestion. J. Agric. Food Chem. 36; 737-741.

Reeck, G. R., De Haen, C., Teller, D. C., Doolittle, R. F., Fitch, W. M., Dickerson, R. E., Chambon, P., McLachlan, A. D., Margoliash, E., Jukes, T. H., and Zuckerkandl, E. (1987). Homology in proteins and nucleic acids: a terminology muddle and a way out of it. Cell 50; 667.

Reed, R. G., Feldhoff, R. C., Clute, O. L., and Peters, T., Jr. (1975). Fragments of Bovine Serum Albumin Produced by Limited Proteolysis. Conformation and Ligand Binding. Biochemistry 14; 4578-4583.

Reed, R.G., Putnam, F.W. and Peters, T. Jr. (1980). Sequence of residues 400-403 of bovine serum albumin. Biochem. J. 191;867-868.

Rees, D. A. and Welsh, E. J. (1977). Secondary and tertiary structure of polysaccharides in solutions and gels. Angew. Chem. Int. Ed. Engl. 16; 214-224.

Reynolds, J. A., Herbert, S., Polet, H. and Steinhardt, J. (1967). The Binding of Divers Detergents Anions to Bovine Serum Albumin. Biochemistry 6; 937-947.

Rice, S. A., Wada, A., and Geidushek, E. P. (1958). Some comments on the Theory of Denaturation. Discuss. Faraday Soc. 25; 130.

Richardson, J. S. (1977). b-sheet topology and the relatedness of proteins. Nature (London) 268; 495-500.

Richardson, J. S. The Anatomy and Taxonomy of Protein Structure. (1981). Adv. protein Chem. 34; 167-339.

Richardson, K. S. C., Nowaczynski, W., and Genest, J. (1977). Specific Aldosterone-Binding Proteins in Human Plasma: Partial Characterisation. J. Steroid Biochem. 8; 951-957.

Richardson, R.K. and Ross-Murphy, S.B. (1981). Mechanical properties of globular protein gels: I. Incipient gelation behaviour. Int. J. Biol. Macromol. 3; 315-322.

Riley, D. P. and Arndt, U. W. (1952). New Type of X-ray Evidence on the molecular structure of Globular Proteins. Nature 169; 138.

Riley, D. P. and Arndt, U. W. (1953). X-Ray Scattering by some native and denatured Proteins in the solid state. Proc. Roy. Soc. B. 141; 93-97

Robbins, R. M. and Holmes, L. G. (1970). Circular dichroism spectra of alpha-lactalbumin. Biochim. Biophys. Acta, 221; 234.

Robinson, A. B. and Rudd, C. (1974). Deamidation of glutaminyl and asparaginyl residues in peptides and proteins. Curr. Top. Cell. Reg. 8; 248.

Roda, A., Cappelleri, G., Aldini, R., Roda, E., and Barbara, L. (1982). Quantitative aspects of the interaction of bile acids with human serum albumin. J. Lipid Res. 23;2 490-495.

Ross-Murphy, S.B. (1991). Physical gelation of synthetic and biological macromolecules. In: "Polymer Gels; Fundamentals and Biomedical Applications". pp. 21-40 (Eds. D.DeRossi, K. Kajiwara, Y. Osada and A. Yamauchi). New York; Plenum Press.

Ross, S. (1950). The Inhibition of Foaming. Rensselaer Polytechnic Institute, Engineering and Science Series No. 63, Troy, New York. pp. 7-9.

Ross, S. and Morrison, I. D. (1988). Colloidal systems and Interfaces. Wiley-Interscience Pub., New York.

Ruegg, M., Moor, U. and Blanc, B. (1977). A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate. J. Dairy Res. 44; 509-520

Russo, P. S. (1987). A perspective on reversible gels and related systems. ACS Symp. Series 350; American Chemical Society, Washington, D. C.

Sakamoto, S. (1973). Patterns of phylogenetic differentiation in the tribe Triticeae. Seiken Ziho 24; 11.

Savu, L., Benassasyag, C., Vallette, G., Christeff, N., and Nuney, E. (1981). Mouse a1 - Fetoprotein and Albumin. J. Biol. Chem. 256; 9414-9418.

Sawyer, L. (1987). One fold among many. Nature(London). 327; 659.

Sawyer, W. H. (1968). Heat denaturation of bovine beta-lactoglobulin and the relevance of disulphide aggregation. J. Dairy Sci. 51; 323-329.

Sayle, R. and Bissell, A. (1993). RasMol: A Program for Fast, Realistic Rendering of Molecular Structures with Shadows. In:"Proceedings of the 10th. Eurographics UK 92 Conference", University of Edinburgh, Scotland.

Scheets, K., Rafalski, J. A. Hedgcoth, C. and Soll, D. G. (1985). Heptapeptide repeat structure of a wheat gamma-gliadin. Pl. Sci. Lett. 37; 221-225

Scheraga, H. (1961). Protein Structure. In: "Molecular Biology Vol. I" (Ed. Kaplan, N. O. and Scheraga, H. A.), Academic Press, New York.

Schmidt, R.H. and Illingworth, B.L. (1978). Gelation properties of whey protein and blended protein systems. Food Product Development 12(10); 60-64.

Schmidt, R. (1981). Gelation and Coagulation. ACS Symp. Ser. 147; 131

Schoen, H. M. (1977). Functional properties of proteins and their measurement. In "Food Proteins" (Eds. Whitaker, J. R. and Tannenbaum, S. R.), p.387. AVI Publ., Westport, Connecticut.

Schofield, J. D., Bottomley, R. C., Timms, M. F. and Booth, M. R. (1983). The effect of heat on wheat gluten and the involvement of sulphydryl-disulphide interchange reaction. J. Cereal Sci. 1; 241-253.

Schulz, G.E. and Schirmer, R.H. (1979). Principles of Protein Structure. Springer-Verlag, Berlin and New York.

Schulz, G. E. and Schirmer, R. H. (1990). Principles of Protein Structure. In: "Springer Advanced Texts in Chemistry". (Ed. C. R. Cantor), Springer-Verlag, New York

Sears, E.R. (1969). Wheat cytogenetics. Ann. Rev. Genet. 3;3 451-468.

Sellers, P. (1974). On the theory and computation of evolutionary distances. SIAM J. Appl. Math. 26; 787-793

Selsted, M. E. and Martinez, R. J. (1980). A simple and ultrasensitive Enzymatic Assay for the Quantitative Determination of Lysozyme in the Picogram Range. Analytical Biochemistry 109; 67-70

Sengupta, C., DeLuca, V., Bailey, D.S. and Verma, D.P.S. (1981). Post- translational processing of 7S and 11S components of soybean storage proteins. Plant Mol. Biol. 1; 19-34.

Sennett, P and Olivier, J. P. (1965). Colloidal Dispersions, Electrokinetic Effects, and the Concept of Zeta Potential. In: "Chemistry and Physics of Interfaces". American Chemical Society, Washington, D. C. USA.

Sharon, N and Lis, H. (1982). In: "The Proteins Vol.5", 3rd. Ed. (Neurath, H. and Hill, R. L. eds.), pp. 1-144, Academic Press.

Shaw, D. J. (1986). Introduction to Colloid and Surface Chemistry. Butterworths, London.

Shewale, J. G., Sinha, S. K. and Brew, K. (1984). Evolution of alpha-lactalbumins. The complete amino acid sequence of alpha-lactalbumin from a marsupial (Macropus rufogriseus) and corrections to regions of sequence in bovine and goat alpha-lactalbumin. J. Biol. Chem. 259; 4947-4956.

Shewry, P.R., Tatham, A.S., Forde, J., Kreis, M. and Miflin, B.J. (1986). The classification and nomenclature of wheat gluten proteins: a reassessment. J. Cer. Sci. 4; 97-106.

Shewry, P. R., Halford, N. G., Field, J. M., and Tatham, A. S. (1989). The structure and functionality of wheat gluten proteins. Proc. Aust. cereal Chem. Conf., 38th. (Murray, L. ed.), R. Aust. Chem. Inst., Melbourne.

Shewry, P.R. (1993). Biological and evolutionary aspects of cereal seed storage proteins. Eds. P.R. Shewry and K.Stobart. In: "Seed Storage Compounds:Biosynthesis, Interactions, and Manipulations". Clarendon Press. Oxford

Shoup, F.K., Pomeranz, Y. and Deyoe, C.W. (1966). Amini acid composition of wheat varieties and flours varying widely in bread-making potentialities. J. Food Sci. 31; 94-101.

Shukla, T. P. (1973). Chemistry and biological function of alpha-lactalbumin. CRC Critical Reviews in Food Technology, 3(3); 241.

Sjoholm, I. and Ljungstedt, I. (1973). Studies on the Tryptophan and Drug-binding Properties of Human Serum Albumin Fragments by affinity chromatography and circular dichroism measurements. J. Biol. Chem. 248; 8434-8441.

Sklar, L. A., Hudson, B. S. and Simoni, R. D. (1975). Conjugated Polyene Fatty Acids as Membrane Probes: Preliminary Characterization. Proc. Nat. Acad. Sci. USA 72; 1649-1653.

Sklar, L. A., Hudson, B. S. and Simoni, R. D. (1976). Conjugate polyene fatty acids as fluorescent membrane probes: model system studies. J. Supramolecular Structure 4; 449-465.

Sklar, L. A., Hudson, B. S. and Simoni, R. D. (1977a). Conjugated Polyene Fatty Acids as Fluorescent Probes: Synthetic Phospholipid Membrane Studies. Biochemistry 16; 819-828.

Sklar, L. A., Hudson, B. S. and Simoni, R. D. (1977b). Conjugated Polyene Fatty Acids on Fluorescent Probes: Spectroscopic Characterization. Biochemistry 16; 813-818.

Sklar, L. A., Hudson, B. S. and Simoni, R. D. (1977c). Conjugate polyene fatty acids as fluorescent membrane probes. Biochemistry 16; 5100-5108.

Smith, J.S.C., and Lester, R.N. (1980). Biochemical systematics and evolution of Zea, Tripsacum, and related genera. Econ. Bot. 34; 201.

Spector, A. A. and Fletcher, J. E. (1978). In: "Disturbances in Lipid and Lipoprotein Metabolism" (Eds. J. M. Dietschy, A. M. Gotto, Jr., and J. A. Ontko). pp. 229-248. Am. Physiol. Soc., Rockville, MD.

Spena, A., Viotti, A. and Pirrotta, V. (1982). A homologous repetitive block structure underlies the heterogeneity of heavy and light chain zein genes. EMBO J. 1; 1589-94.

Spencer, D. and Higgins, T.J.V. (1982). Seed maturation and deposition of storage proteins. In: "The Molecular Biology of Plant Development". ( Ed. H. Smith and D. Grierson). Oxford: Blackwell.

Squire, P. G., Moser, P., and O’Konski, C. T. (1968). The hydrodynamic Properties of Bovine Serum Albumin monomer and Dimer. Biochemistry 7; 4261-4272.

Stainsby, G. (1980). Proteinaceous gelling systems and their complexes with polysaccharides. Food Chemistry 6; 3-14.

Stamler, J. S., Singel, D. J., and Loscalzo, J. (1992). Biochemistry of Nitric Oxide and its Redox-Activated Forms. Science 258; 1898-1902.

Sternberg, M. J. E. and Thornton, J. M. (1976). On the conformation of proteins: The handedness of the beta-strand-alpha-helix-beta-strand unit. J. Mol. Biol. 105; 367-382.

Sternberg, M. J. E. (1991). PROMOT: a FORTRAN program to scan protein sequences against a library of known motifs. Cabios, 7; 257-260.

Stevens, D.J. (1973). Reaction of Wheat Proteins with Sulphite. III. Measurement of Labile and Reactive Disulphide Bonds in Gliadin and in the Protein of Aleurone Cells. J. Sci. Fd. Agric. 24; 279-283.

Stillinger, F. H. and Rahman, A. (1974). Improved simulation of liquid water by molecular dynamics. J. Chem. Phys. 60; 1545-1557.

Stuart, D.I., Acharya, K.R., Walker, N.P.C., Smith, S.G., Lewis, M. and Phillips, D.C. (1986). Alpha-Lactalbumin possesses a novel calcium binding loop. Nature (London). 324; 84-87.

Stuhrmann, H.B. (1974). Neutron small-angle scattering of biological macromolecules in solution. J. Appl. Cryst. 7; 173-178.

Stuhrmann, H. B. and Miller, A. (1978). Small-angle scattering of biological structures. J. Appl. Crystallogr. 11; 325-345.

Suzuki, E., Van Donkelaar, A., Varghese, J.N., Lilley, G.G., Blagrove, R.J., Colman, P.M. (1983). Crystallization of phaseolin from Phaseolus vulgaris. J. Biol. Chem. 258; 2634-36.

Swaisgood, H. E. (1982). Chemistry of milk proteins. In: "Developments in Dairy Chemistry 1". (P.F. Fox, ed.). Vol. 1. Applied Sci., London.

Tanaka, T. (1981). Gels. Sci. Am. 244; 110-123.

Tanford, C. (1968). Protein Denaturation. Adv. Protein Chem. 23; 121-282.

Tanford, C. (1980). The Hydrophobic Effect. Wiley, New York.

Tatham, A. S., Shewry, P. R. and Belton, P. S. (1990a). Structural Studies of Cereal Prolamines, including Wheat Gluten. In: "Advances in Cereal Science and Technology". (Ed. Y. Pomeranz). American Association of Cereal Chemists, USA.

Tatham, A. S. Masson, P. and Popineau, Y. (1990b). Conformational studies of peptides derived from the enzymic hydrolysis of a gamma-type gliadin. J. Cereal Sci. 11; 1-13.

Taylor N. W. and Cluskey, J. E. (1962). Wheat gluten and its glutenin component: Viscosity, diffusion and sedimentation studies. Arch. Biochem. Biophys. 97; 399-405.

Taylor, W. and Thorton, J. (1984). Recognition of super-secondary structure in proteins. J. Mol. Biol. 173; 487-514.

Thomson, N. H., Miles, M. J., Tatham, A. S. and Shewry, P. R. (1992). Molecular images of cereal prolamines by STM. Ultramicroscopy 42-44; 1204-1213

Thornton, J. M. (1981). Disulphide Bridges in Globular Proteins. J. Mol. Biol. 151; 261-287.

Timasheff, S. N. and Townend, R. (1964). Structure of the beta-Lactoglobulin Tetramer. Nature 203; 517-519.

Timasheff, S. N., and Gibbs, R. J. (1957). The state of plasma albumin in acid pH. J. Archs. Biochem. Biophys. 70; 547-560.

Tolstoguzov, V. B. (1986). Functional properties of proteins-polysaccharide mixtures. In "Functional properties of Food Macromolecules". (Eds. J. R. Mitchell and D. A. Ledward) p.385. Elsevier. Amsterdam.

Tombs M. P. (1970). Proteins as Human Foods, (Ed. Lawrie, R. A. ). Butterworths, London.

Townsend, A. A. and Nakai, S. (1983). Relationships between hydrophobicity and foaming characteristics of food proteins. J. Food Sci. 48; 588.

Treolar, L. R. G. (1975). The elasticity of a molecular network. In: "The Physics of Rubber Elasticity". Clarendon Press, Oxford. pp. 59-79.

Tucker, E. E., Lane, E. H. and Christian, S. D. (1981). Vapor pressure studies of hydrophobic interactions. Formation of benzene-benzene and cyclohexane-cyclohexanol dimers in dilute aqueous solutions. J. Solut. Chem. 10; 1-20.

Tung, M. A. (1978). Rheology of protein dispersions. J. Texture Stud. 9; 3-31.

Unger, W. G. (1972). Binding of Prostaglandin to human serum albumin. J. Pharm. Pharmacol. 24; 470-477.

Vanaman, T.C., Brew, K. and Hill, R.L. (1970). The Disulphide Bonds of Bovine alpha-Lactalbumin. J.Biol. Chem. 245; 4583-4590.

Van de Kamer, J. H. and Weijers, H. A. (1955). Coeliac disease: some experiments on the cause of the harmful effects of wheat gliadin. Acta Paediatrica 44; 465-469.

van Oers, N. S. C., Cohen, B. L., and Murgita, R. A. (1989). Isolation and characterization of a distinct immunoregulatory isoform of alpha-fetoprotein produced by the normal fetus. J. Exp. Med. 170; 811-825.

Venkatachalam, C. M. (1968). Stereochemical Criteria for Polypeptides and Proteins V: Conformation of a System of three linked Peptide Units. Biopolymers 6; 1425-1436.

Voet, D., and Voet, J. G. (1990). Biochemistry. Wiley, New York

Von Heijne, G. (1983). Patterns of amino acids near signal-sequence cleavage sites. Eur. J. Biochem. 133; 17-21

Waldmann, T. A. (1977). In: "Albumin Structure, Function and Uses". (Eds. V. M. Rosenoer, M. Oratz, and M. A. Rothschild ), pp. 255-273. Pergamon, Oxford.

Walisch,W. and Eberle,H.G. (1967). Mikrochim Acta. 6; 1031.

Walstra, P., van Vliet, T and Bremer, L. G. B. (1991). On the Fractal Nature of Particle Gels. In: "Food Polymers, Gels, and Colloids". (ed. Dickinson, E). Special Publication No. 82, pp. 369-382.

Wang, C-H. and Damodaran, S. (1991). Thermal Gelation of Globular Proteins: Influence of Protein Conformation on Gel Strength. J. Agric. Food Chem. 39; 433-438.

Wang, C.S., Chan, W.Y. and Kloer, H.U. (1984). Comparative studies on the chemical and immunochemical properties of human milk, human pancreatic juice and bovine milk lactoferrin. Comp. Biochem. Physiol. 78B; 575.

Warrant, R. W. and Kim, S-H. (1978). Alpha-Helix-double helix interaction shown in the structure of a protamine-transfer RNA complex and a nucleoprotamine model. Nature 271; 130.

Wasserman, P. M. (1987). Early events in mammalian fertilization. Annu. Rev. Cell Biol. 3; 109-142.

Watanabe, K. and Klostermeyer, H. (1976). Heat induced changes in sulphydryl and disulphide levels of beta-lactoglobulin A and the formation of polymers. J. Dairy Res. 43; 411-418.

Watenpaugh, K. D., Sieker, L. C. and Jensen, L. (1979). The Structure of Rubredoxin at 1.2Å Resolution. J. Mol. Biol. 131; 509-522.

Weber, E., and Neumann, D. (1980). Protein bodies, storage organelles in plant seeds. Biochem. Physiol. Pflanz. 175; 279-306.

Webster, B. (1990). Chemical Bonding Theory. Blackwell Scientific Pub. Oxford

Werner, A. (1893). Beitrag zur Konstitution anorganischer Verbindungen, Z. Anorg. Allg. Chem. 3; 267-342. [ Translated into English in Kauffman, G.B. (1968). "Classics in Coordination Chemistry, Part 1: The selected Papers of Alfred Werner" pp. 5-88. Dover, New York.]

Westphal, U., and Harding, G. B. (1973). Steroid-Protein Interactions. XXVII. Progesterone Binding to Polymers of Human Serum Albumin. Biochim. Biophys. Acta 310; 518-527.

Wetlaufer, D. B. (1973). Nucleation, rapid folding, and globular intrachain regions in proteins. Proc. Nat. Acad. Sci. USA 70; 697-701.

Wetlaufer, D. B. and Ristow, S. (1973). Acquisition of three-dimensional structure of proteins. Ann. Rev. Biochem. 42; 135-158.

Wetzel, R., Becker, M., Behlke, J., Billwitz, H., Bohm, S., Ebert, B., Hamann, H., Krumbiegel, J. and Lasmann, G. (1980). Temperature Behaviour of Human Serum Albumin. Eur. J. Biochem. 104; 469-478.

Whitney, R.., Brunner, J. R., Ebner, K. E., Farrell, H. M., Josephson, R.V., Morr, C. V. and Swaisgood, H. E. (1976). Nomenclature of the proteins of cow's milk: Fourth Revision. J. Dairy Sci. 59; 795- 815.

Whitney, R. McL., Brunner, J. R., Ebner, K. E., Farrell, H. M., Jr., Josephson, R. V., Morr, C. V., and Swaisgood, H. E. (1976). J. Dairy Sci. 59; 785.

Williams, S. (1984). Official Methods of Analysis of Association Chemicals, edition 14. AOAC, Virginia

Windsor, C. G. (1981). Pulse Neutron Scattering. Taylor and Francis, London

Wong, K. P. and Tanford, C. (1973). Denaturation of bovine carbonic anhydrase-B by guanidine hydrochloride. A process involving separable sequential conformational transitions. J. Biol. Chem. 248; 8518.

Woychick, J.H., Boundy, J. A. and Dimler, R. J. (1961). Starch gel electrophoresis of wheat gluten proteins with concentrated urea. Arch. Biochem. Biophys. 94; 477-482.

Wright, A. K., and Thompson, M. R. (1975). Hydrodynamic structure of Bovine Serum Albumin determined by Transient Electric Birefringence. Biophys. J. 15; 137-141.

Wright, D.J., Leach, I.B., and Wilding, P. (1977). Differential scanning calorimetric studies of muscles and its constituent proteins. J.Sci. Food Agric. 28; 557

Wright, D.J. (1984). Thermoanalytical methods in food research. In : "Biophysical Methods in Food Research". Ed. H.W.S.Chan. Blackwell, London

Wright H. T. (1973). Comparison of the Crystal Structures of Chymotrypsinogen-A and alpha-Chymotrypsin. J. Mol. Biol. 79; 1-23.

Wright, H. T. and Robinson, A. B. (1982). Cryptic amidase active sites catalyze deamidation in proteins. In: "From Cyclotrons to Cytochromes". (Eds. Kaplan, N. O. and Robinson, A. B.), Academic Press, New York.

Wrigley, C.W., and Shepherd, K.W. (1973). Electrofocusing of grain proteins from wheat genotypes. Ann. N.Y. Acad. Sci. 209; 154-162.

Wu C. H., Shuryo, N. and Powrie, W. D. (1976). Preparation and properties of acid solubilized gluten. J. Agric. Food Chem. 24; 504-510.

Wu Y. V. and Dimler, R. J. (1964). Conformational studies of wheat gluten, glutenin and gliadin in urea solutions at various pHs. Arch. Biochem. Biophys. 107; 435-440.

Wyckoff, R. W. G. and Posnjak, E. (1921). The crystal structure of ammonium chloroplatinate. J. Am. Chem. Soc. 43; 2291-2309.

Yamashita, M.M., Wesson, L., Eisenman, G., and Eisenberg, D. (1990). Where metal ions bind in proteins. Proc. Natl. Acad. Sci. USA. 87; 5648-5652.

Yang, J. T. (1961). The Viscosity of Macromolecules in Relation to Molecular Conformation. Adv. Protein Chem. 16; 323-400

Yang, J. T., Wu, C. S. C. and Martinez, H. M. (1986). Calculation of Protein Conformation from Circular Dichroism. Meth. Enzymol. 130; 208-269.

Yates, F. E. and Urguhart, J. (1962). Control of Plasma concentrations of Adrenocortical Hormones. Physiol. Rev. 42; 359-443.

Ziegler, G. R. and Foegeding, E. A. (1990). The Gelation of Proteins. Adv. Food Nutri. Res. 34; 203-298.

Zuckerkandl, E. (1975). The appearance of new structures and functions in proteins during evolution. J. Mol. Evol. 7; 1-57.

Zvelebil, M. J., Barton, G. J. Taylor, W. R. and Sternberg, M. J. E. (1987). Prediction of protein secondary structure and active sites using the alignment of homologous sequences. J. Mol. Biol. 195; 957-961.