@misc{gamow1956problem8,
    author = "Gamow, G. and Rich, A. and Yas, M",
    title = "Problem of information transfer from nucleic acids to proteins",
    year = "1956",
    howpublished = "Advances in Biological and Medical Physics, v. 4, p. 23-68",
    note = "talkorigins\_source = {true}; raw\_reference = {Gamow, G., Rich, A., and Yas, M., 1956, Problem of information transfer from nucleic acids to proteins: Advances in Biological and Medical Physics, v. 4, p. 23-68.}"
}

@article{doi101126science12833331214,
    author = "FOX, S W and HARADA, K",
    title = "Thermal copolymerization of amino acids to a product resembling protein.",
    year = "1958",
    journal = "Science (New York, N.Y.)",
    url = "https://pubmed.ncbi.nlm.nih.gov/13592311/",
    doi = "10.1126/science.128.3333.1214",
    pmid = "13592311"
}

@article{fox1958thermal,
    author = "Fox, Sidney W. and Harada, Kaoru",
    title = "Thermal Copolymerization of Amino Acids to a Product Resembling Protein",
    year = "1958",
    journal = "Science",
    url = "https://doi.org/10.1126/science.128.3333.1214",
    doi = "10.1126/science.128.3333.1214",
    number = "3333",
    pages = "1214-1214",
    volume = "128"
}

@misc{fox1958thermal5,
    author = "Fox, S. W. and Harada, K",
    title = "Thermal copolymerization of amino acids to a product resembling protein",
    year = "1958",
    howpublished = "Science, v. 128, p. 1214",
    note = "talkorigins\_source = {true}; raw\_reference = {Fox, S. W., and Harada, K., 1958, Thermal copolymerization of amino acids to a product resembling protein: Science, v. 128, p. 1214.}"
}

@article{fox1960the,
    author = "Fox, Sidney W. and Harada, Kaoru",
    title = "The Thermal Copolymerization of Amino Acids Common to Protein 1",
    year = "1960",
    journal = "Journal of the American Chemical Society",
    url = "https://doi.org/10.1021/ja01499a069",
    doi = "10.1021/ja01499a069",
    number = "14",
    pages = "3745-3751",
    volume = "82"
}

@article{fox1960thermal,
    author = "Fox, Sidney W. and Harada, Kaoru",
    title = "Thermal copolymerization of amino acids in the presence of phosphoric acid",
    year = "1960",
    journal = "Archives of Biochemistry and Biophysics",
    url = "https://doi.org/10.1016/0003-9861(60)90419-7",
    doi = "10.1016/0003-9861(60)90419-7",
    number = "2",
    pages = "281-285",
    volume = "86"
}

@article{doi101038195385a0,
    author = "KRAMPITZ, G and KNAPPEN, F",
    title = "Thermal copolymerization of protein hydrolysates containing 35S amino-acids and distribution of radioactive sulphur after application of 35S-labelled amino-acid copolymers in the rat.",
    year = "1962",
    journal = "Nature",
    url = "https://pubmed.ncbi.nlm.nih.gov/14459316/",
    doi = "10.1038/195385a0",
    pmid = "14459316"
}

@book{fox1962the6,
    author = "Fox, S. W. and Harada, K. and Rohlfing, D. L",
    title = "The thermal copolymerization of -amino acids, in Stahmann, M. A., ed., Polyamino Acids, Polypeptides, and Proteins",
    year = "1962",
    publisher = "Madison, Wisconsin, University of Wisconsin Press, p. 47-54",
    note = "talkorigins\_source = {true}; raw\_reference = {Fox, S. W., Harada, K., and Rohlfing, D. L., 1962, The thermal copolymerization of -amino acids, in Stahmann, M. A., ed., Polyamino Acids, Polypeptides, and Proteins: Madison, Wisconsin, University of Wisconsin Press, p. 47-54.}"
}

@incollection{vegotsky1962protein10,
    author = "Vegotsky, A. and Fox, S. W",
    editor = "Florkin, M. and Mason, H. S.",
    title = "Protein molecules: intraspecific and interspecific variations",
    year = "1962",
    booktitle = "Comparative Biochemistry",
    publisher = "New York, Academic Press, v. IV, p. 185-224",
    note = "talkorigins\_source = {true}; raw\_reference = {Vegotsky, A., and Fox, S. W., 1962, Protein molecules: intraspecific and interspecific variations, in Florkin, M., and Mason, H. S., eds., Comparative Biochemistry: New York, Academic Press, v. IV, p. 185-224.}"
}

@misc{fox1963abiotic7,
    author = "Fox, S. W. and Yuyama, S",
    title = "Abiotic production of primitive protein and formed microparticles",
    year = "1963",
    howpublished = "Annals of the New York Academy of Sciences, v. 108, p. 487-494",
    note = "talkorigins\_source = {true}; raw\_reference = {Fox, S. W., and Yuyama, S., 1963, Abiotic production of primitive protein and formed microparticles: Annals of the New York Academy of Sciences, v. 108, p. 487-494.}"
}

@book{fox1965experiments3,
    author = "Fox, S. W",
    title = "Experiments suggesting evolution to protein, in Bryson, V., and Vogel, H. J., eds., Evolving Genes and Proteins",
    year = "1965",
    publisher = "New York, Academic Press, p. 359-369",
    note = "talkorigins\_source = {true}; raw\_reference = {Fox, S. W., 1965, Experiments suggesting evolution to protein, in Bryson, V., and Vogel, H. J., eds., Evolving Genes and Proteins: New York, Academic Press, p. 359-369.}"
}

@misc{hayakawa1967copolymerization9,
    author = "Hayakawa, T. and Windsor, C. R. and Fox, S. W",
    title = "Copolymerization of the Leuchs anhydrides of the eighteen amino acids common to protein",
    year = "1967",
    howpublished = "Archives of Biochemistry and Biophysiology, v. 118, p. 265-272",
    note = "talkorigins\_source = {true}; raw\_reference = {Hayakawa, T., Windsor, C. R., and Fox, S. W., 1967, Copolymerization of the Leuchs anhydrides of the eighteen amino acids common to protein: Archives of Biochemistry and Biophysiology, v. 118, p. 265-272.}"
}

@misc{dayhoff1969atlas1,
    author = "Dayhoff, M. O",
    title = "Atlas of Protein Sequence and Structure",
    year = "1969",
    howpublished = "Silver Spring, Md., National Biomedical Research Foundation, v. 4",
    note = "talkorigins\_source = {true}; raw\_reference = {Dayhoff, M. O., 1969, Atlas of Protein Sequence and Structure: Silver Spring, Md., National Biomedical Research Foundation, v. 4.}"
}

@misc{dayhoff1972atlas2,
    author = "Dayhoff, M. O",
    title = "Atlas of Protein Sequence and Structure",
    year = "1972",
    howpublished = "Sliver Spring, Md., National Biomedical Research Foundation, v. 5",
    note = "talkorigins\_source = {true}; raw\_reference = {Dayhoff, M. O., 1972, Atlas of Protein Sequence and Structure: Sliver Spring, Md., National Biomedical Research Foundation, v. 5.}"
}

@article{doi101016030326477690006x,
    author = "Fox, S W and Suzuki, F",
    title = "Linkages in thermal copolymers of lysine.",
    year = "1976",
    journal = "Bio Systems",
    abstract = "The thermal copolymerization of lysine with other alpha-amino acids has been studied further. The identity of the second amino acid influences various properties of the polymer obtained, including the proportion of alpha and epsilon linkages of lysine. A review of linkages in proteinoids indicated alpha and beta linkages for aspartic acid, alpha and gamma linkages for glutamic acid, alpha and epsilon linkages for lysine, and alpha linkages for other amino acids. Thermal proteinoids are thus more complex in types of linkage than are proteins.",
    url = "https://pubmed.ncbi.nlm.nih.gov/953158/",
    doi = "10.1016/0303-2647(76)90006-x",
    pmid = "953158"
}

@article{doi101021ma60060a021,
    author = "Konishi, Y and van Nispen, J W and Davenport, G and Scheraga, H A",
    title = "Helix-coil stability constants for the naturally occurring amino acids in water. 15 Arginine parameters from random poly(hydroxybutylglutamine-co-L-arginine).",
    year = "1977",
    journal = "Macromolecules",
    abstract = "Water-soluble copolymers containing L-arginine and N5-(4-hydroxybutyl)-L-glutamine were prepared by copolymerization of the N-carboxy-alpha-amino acid anhydrides of Ndelta-tert-butyloxycarbonyl-L-ornithine and gamma-benzyl L-glutamate, followed by aminolysis with 4-amino-1-butanol, by removal of the tert-butyloxycarbonyl protecting group, and by treatment with O-methylisourea. The copolymers were fractionated and characterized, and the thermally induced helix-coil transitions of these copolymers were studied in water at neutral pH in the presence and in the absence of KCl. The Zimm-Bragg parameters sigma and s for the helix-coil transition in poly(L-arginine) in aqueous solution were deduced from an analysis of the melting curves of the copolymers in the manner described in earlier papers. The computed values of s indicate that L-arginine is a weak helix-making residue at low temperature and a weak helix-breaking residue at high temperature in aqueous solution. The results were found to be in good agreement with those obtained earlier in conformational analyses of arginyl residues in proteins.",
    url = "https://pubmed.ncbi.nlm.nih.gov/926821/",
    doi = "10.1021/ma60060a021",
    pmid = "926821"
}

@phdthesis{fox1981origins4,
    author = "Fox, S. W",
    title = "Origins of the protein synthesis cycle",
    year = "1981",
    publisher = "International Journal of Quantum Chemistry, v. QBS8, p. 441-454",
    note = "talkorigins\_source = {true}; raw\_reference = {Fox, S. W., 1981, Origins of the protein synthesis cycle: International Journal of Quantum Chemistry, v. QBS8, p. 441-454.}"
}

@article{doi1010160303264787900281,
    author = "Vaughan, G and Przybylski, A T and Fox, S W",
    title = "Thermal proteinoids as excitability-inducing materials.",
    year = "1987",
    journal = "Bio Systems",
    abstract = "The deposition of thermal copolyamino acids on planar lipid membranes causes oscillations and action potentials upon electrical stimulation. Results are reported for compositionally simple thermal copoly(asp,glu) and for a more heterotonic polyamino acid. The data conform to the interference that electrical activity of cellular membranes is due to the polypeptide components, not to the lipid components. Because of the ease and controllability of producing polypeptides by thermal copolymerization of amino acids, new possibilities in investigation of structure-excitability relationships are provided.",
    url = "https://pubmed.ncbi.nlm.nih.gov/3620604/",
    doi = "10.1016/0303-2647(87)90028-1",
    pmid = "3620604"
}

@article{doi101016001670379500037z,
    author = "Fox, S W",
    title = "Thermal synthesis of amino acids and the origin of life.",
    year = "1995",
    journal = "Geochimica et cosmochimica acta",
    abstract = "The recent review by Marshall (1994) of the production of amino acids from the interstellar components, formaldehyde and ammonia, is placed in the larger context of the origin of life. Thermal energy, being ubiquitous in the Earth, emerges as the sole necessary form of energy. To appreciate the overview of the natural evolutionary sequence it is necessary to recognize stepwiseness in evolution, a principle that has however been often ignored. Since self organization of thermal protein to cells is instantaneous, but only one step in a geochemical ladder, individual steps may be regarded as instantaneous, while the sequence requires measurable time. Two steps indicated are extrusion of a hot, dry organic magma of amino acids --> peptides into an aqueous environment in which occurs a second step of self organization. In this paper, spinoffs of the defensible theory for the origin of life have been briefly reviewed as a fundamental consequence of nonrandom thermal copolymerization of amino acids.",
    url = "https://pubmed.ncbi.nlm.nih.gov/11540049/",
    doi = "10.1016/0016-7037(95)00037-z",
    pmid = "11540049"
}

@article{crossref2009protein,
    title = "PROTEIN SPARING PRODUCED BY PROTEINS AND AMINO ACIDS",
    year = "2009",
    journal = "Nutrition Reviews",
    url = "https://doi.org/10.1111/j.1753-4887.1976.tb05750.x",
    doi = "10.1111/j.1753-4887.1976.tb05750.x",
    number = "6",
    pages = "174-176",
    volume = "34"
}