Abstract
At one point in the history of protein chemistry it was thought that—because of the vast number of possible sequences—proteins ought to exist in a countless number of forms befitting any conceivable function or structure. In fact, as the number of known amino acid sequences continues to mount, it is becoming abudantly clear that there is a practical limit to the number of types of protein structures that exist in living systems on Earth. Thus, although the number of possible sequences for 20 amino acids arranged randomly in strings of 350 units is a superastronomical 20350, certainly nowhere near that number of protein sequences has ever or will ever exist. Instead, a small number of genetically encoded protein structures has been expanded by the general route of “duplication and modification.” The duplications come in various degrees, from the very short to the supragenic or chromosomal. Postduplication modification mostly takes the form of base substitutions leading to amino acid replacement, and, theoretically, the history of any protein ought to be evident by appropriate comparison of the diverging sequences.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Argraves, W. S., Deak, F., Sparks, K. J., Kiss, I., and Goetinck, P. F., 1987, Structural features of cartilage matrix protein deduced from cDNA, Proc. Natl. Acad. Sci. U.S.A. 84:464–468.
Banyai, L., Varadi, A., and Patthy, L., 1983, Common evolutionary origin of the fibrin-binding structures of fibronectin and tissue-type plasminogen activator, FEBS Lett. 163:37–41.
Barnett, D. R., Lee, T. H., and Bowman, B. H., 1972, Amino acid sequence of the human haptoglobin ß chain. Amino-and carboxyl-terminal sequences, Biochemistry 11:1189–1194.
Bentley, D. R., 1986, Primary structure of human complement component C2, Biochem. J. 239:339–345.
Black, J. A., and Dixon, G. H., 1967, Evolution of protamine: A further example of partial gene duplication, Nature 216:152–154.
Black, J. A., Harkins, R. N., and Stenzel, P., 1976, Non-random relationships among amino acids in protein sequences, Int. J. Peptide Protein Res. 8:125–130.
Bock, S. C., Shriver, K., Nielson, E., Thogersen, H.-C., Wiman, B., Donaldson, V. H., Eddy, R. L., Marrinan, J., Radziejewska, E., Huber, R., Shows, T. B., and Magnusson, S., 1986, Human C1 inhibitor: Primary structure, cDNA cloning, and chromosomal localization, Biochemistry 25:4292–4301.
Brew, K., Vanaman, T. C., and Hill, R. L., 1967, Comparison of the amino acid sequence of bovine α-lactalbumin and hens eggwhite lysozyme, J. Bioi. Chem. 242:3747–3749.
Broglie, K. E., Gaynor, J. J., and Broglie, R. M., 1986, Ethylene-regulated gene expression: Molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris, Proc. Natl. Acad. Sci. U.S.A. 83:6820–6824.
Büchel, D. E., Gronenborn, B., and Müller-Hill, B., 1980, Sequence of the lactose permease gene, Nature 283: 541–545.
Byrne, B. M., van het Schip, A. D., van de Klundert, J. A. M., Arnberg, A. C., Gruber, M., and Geert, A. B., 1984, Amino acid sequence of phosvitin derived from the nucleotide sequence of part of the chicken vitellogenin gene, Biochemistry 23:4275–4279.
Carrell, R. W., Jeppsson, J.-O., Laurell, C.-B., Brennan, S. O., Owen, M. C., Vaughan, L., and Boswell, D. R., 1982, Structure and variation of human α1-antitrypsin, Nature 298:329–334.
Chandra, T., Stackhouse, R., Kidd, V. J., Robson, K. J. H., and Woo, S. L. C., 1983a, Sequence homology between human α1-antichymotrypsin, α1-antitrypsin, and antithrombin III, Biochemistry 22:5055–5061.
Chandra, T., Stackhouse, R., Kidd, V. J., and Woo, S. L. C., 1983b, Isolation and sequence characterization of a cDNA clone of human antithrombin III, Proc. Natl. Acad. Sci. U.S.A. 80:1845–1848.
Chou, P. Y., and Fasman, G. D. 1974, Prediction of protein conformation, Biochemistry, 13:222–245.
Chou, P. Y.,and Fasman, G. D., 1978, Empirical prediction of protein conformation, Annu. Rev. Biochem. 47: 251–276.
Chung, L. P., Bentley, D. R., and Reid, K. B. M., 1985, Molecular cloning and characterization of the cDNA coding for C4b-binding protein, a regulatory protein of the classical pathway of the human complement system, Biochem. J. 230:133–141.
Coelingh, J. P., Monfoort, C. H., Rozijn, T. H., Gevers Leuven, J. A., Schiphof, R., Steyn-Parve, E. P., Braunitzer, G., Schrank, B., and Ruhfus, A., 1972, The complete amino acid sequence of the basic nuclear protein of bull spermatozoa, Biochim. Biophys. Acta 285:1–14.
Davie, E. W., Ichinose, A., and Leytus, S. P., 1986, Structural features of the proteins participating in blood coagulation and fibrinolysis, Cold Spring Harbor Symp. Quant. Biol. 51:509–514.
Dayhoff, M. O., 1978, Atlas of Protein Sequence and Structure, Volume 5, Suppl. 3, National Biomedical Research Foundation, Washington.
DeVries, A. L., Vandenheede, J., and Feeney, R. E., 1972, Primary structure of freezing point-depressing glycoproteins, J. Biol. Chem. 246:305–308.
DiScipio, R. G., Gehring, M. R., Podack, E. R., Kan, C. C., Hugli, T. E., and Fey, G. H., 1984, Nucleotide sequence of cDNA and derived amino acid sequence of human complement component C9, Proc. Natl. Acad. Sci. U.S.A. 81:7298–7302.
Dixon, R. A. F., Kobilka, B. K., Strader, D. J., Benovic, J. L., Dohlman, H. G., Frielle, T., Bolanowski, M. A., Bennett, C. D., Rands, E., Diehl, R. E., Mumford, R. A., Slater, E. E., Sigal, I. S., Caron, M. G., Lefkowitz, R. J., and Strader, C. D., 1986, Cloning of the gene and cDNA for mammalian ß-adrenergic receptor and homology with rhodopsin, Nature 321:75–79.
Doolittle, R. F., 1979, Protein evolution, in: The Proteins (H. Neurath and R. L. Hill, eds.), 2nd ed., Volume 4, Academic Press, New York, pp. 1–118.
Doolittle, R. F., 1981, Similar amino acid sequences: Chance or common ancestry? Science 214:149–159.
Doolittle, R. F., 1983, Angiotensinogen is related to the antitrypsin-antithrombin-ovalbumin family, Science 222:417–419.
Doolittle, R. F., 1985, The genealogy of some recently evolved vertebrate proteins, Trends Biochem. Sci. 10: 233–237.
Doolittle, R. F., 1986a, Protein sequence data banks: The continuing search for related structures, in: Protein Engineering (M. Inouye, ed.), Academic Press, Orlando, FL, 15–27.
Doolittle, R. F., 1986b, Of URFs and ORFs: A Primer on How to Analyze Derived Amino Acid Sequences, University Science Books, Mill Valley, CA.
Doolittle, R. F., Watt, K. W. K., Cottrell, B. A., Strong, D., and Riley, M., 1979, Amino acid sequence of the α-chain of human fibrinogen, Nature 280:464–468.
Doolittle, R. F., Woodbury, N. W., and Jue, R. A., 1982, Ribosomal protein S1 is the product of a series of contiguous duplications, Biosci. Rep. 2:405–412.
Doolittle, R. F., Feng, D.-F., and Johnson, M. S., 1984, Computer-based characterization of epidermal growth factor precursor, Nature 307:558–560.
Doolittle, R. F., Feng, D.-F., Johnson, M. S., and McClure, M. A., 1986, Relationships of human protein sequences to those of other organisms, Cold Spring Harbor Symp. Quant. Biol. 51:447–455.
Eck, R. V., and Dayhoff, M. O., 1966, Evolution of the structure of ferredoxin based on living relics of primitive amino acid sequences, Science 152:363–366.
Eckert, R. L., and Green, H., 1986, Structure and evolution of the human involucrin gene, Cell 46:583–589.
Enfield, D. L., Ericsson, L. H., Fujikawa, K., Walsh, K. A., Neurath, H., and Titani, K., 1980, Amino acid sequence of the light chain of bovine factor X, Biochemistry 19:659–667.
Feng, D. F., Johnson, M. S., and Doolittle, R. F., 1985, Aligning amino acid sequences: Comparison of commonly used methods, J. Mol. Evol. 21:112–125.
Fernlund, P., Stenflo, J., and Tufvesson, A., 1978, Bovine protein C: Amino acid sequence of the light chain, Proc. Natl. Acad. Sci. U.S.A. 75:5889–5892.
Flink, I. L., Bailey, T. J., Gustafson, T. A., Markham, B. E., and Morkin, E., 1986, Complete amino acid sequence of human thyroxine-binding globulin deduced from closed DNA: Close homology to the serine antiproteases, Proc. Natl. Acad. Sci. U.S.A. 83:7708–7712.
Friden, P., Newman, T., and Freundlich, M., 1982, Nucleotide sequence of the ilvB promoter-regulatory region: A biosynthetic operon controlled by attenuation and cyclic AMP, Proc. Natl. Acad. Sci. U.S.A. 79: 6156–6160.
Gamow, G., Rich, A., and Ycas, M., 1956, The problem of information transfer from the nucleic acids to proteins, Adv. Biol. Med. Phys. 4:23–68.
Garfinkel, M. D., Pruitt, R. E., and Meyerowitz, E. M., 1983, DNA sequence, gene regulation and modular protein evolution in the Drosophila 68C glue gene cluster, J. Mol. Biol. 168:765–789.
George, D. L., Scott, A. F., Trusko, S., Glick, B., Ford, E., and Dorney, D., 1985, Structure and expression of amplified cKi-ras gene sequences in Y1 mouse adrenal tumor cells, EMBO J. 4:1199–1203.
Godovac-Zimmermann, J., Conti, A., Liberatori, J., and Braunitzer, G., 1985, The amino-acid sequence of ß-lactoglobulin II from horse colostrum (Equus caballus, Perissodactyla): ß-Lactoglobulins are retinol-binding proteins, Biol. Chem. Hoppe-Seyler 366:601–608.
Green, R. L., and Warren, G. J., 1985, Physical and functional repetition in a bacterial ice nucleation gene, Nature 317:645–648.
Greenwald, I., 1985, lin-12, A nematode homeotic gene, is homologous to a set of mammalian proteins that includes epidermal growth factor, Cell 43:583–590.
Greer, J., 1985, Protein structure and function by comparative model building, Ann. N.Y. Acad. Sci. 439:144–163.
Hagen, D. C., McCaffrey, G., and Sprague, G. F., 1986, Evidence the yeast STE3 gene encodes a receptor for the peptide pheromone a factor: Gene sequence and implications for the structure-of the presumed receptor, Proc. Natl. Acad. Sci. U.S.A. 83:1418–1422.
Hagen, F. S., Gray, C. L., O’Hara, P., Grant, F. J., Saari, G. C., Woodbury, R. G., Hart, C. E., Insley, M., Kisiel, W., Kurachi, K., and Davie, E. W., 1986, Characterization of a cDNA coding for human factor VII, Proc. Natl. Acad. Sci. U.S.A. 83:2412–2416.
Hammond, G. L., Smith, C. L., Goping, I. S., Underhill, D. A., Harley, M. J., Reventos, J., Musto, N. A., Gunsalus, G. L., and Bardin, C. W., 1987, Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors, Proc. Natl. Acad. Sci. U.S.A. 84:5153–5157.
Hampe, A., Gobet, M., Sherr, C. J., and Galibert, F., 1984, Nucleotide sequence of the feline retroviral oncogene v-fms shows unexpected homology with oncogenes encoding tyrosine-specific protein kinases, Proc. Natl. Acad. Sci. U.S.A. 81:85–89.
Hayashida, H., Kuma, K., and Miyata, T., 1988, Immunoglobulin-like sequences in the extracellular domains of proto-oncogene fms and platelet-derived growth factor receptor, Proc. Japan. Acad. 64(Suppl. B): 113–118.
Heck, J. D., and Hatfield, G. W., 1988, Valyl-tRNA synthetase gene of Escherichia coli K12: Primary structure of the valS gene and homology with other aminoacyl-tRNA synthetases, J. Biol. Chem. 263:857–867.
Hejgaard, J., Rasmussen, S. K., Brandt, A., and Svendsen, I., 1985, Sequence homology between barley endosperm protein Z and protease inhibitors of the α1-antitrypsin family, FEBS Lett. 180:89–94.
Hojrup, P., Jensen, M. S., and Petersen, T. E., 1985, Amino acid sequence of bovine protein Z: A vitamin K-dependent serine protease homolog, FEBS Lett. 184:333–338.
Holmquist, R., and Moise, H., 1975, Compositional nonrandomness: A quantitatively conserved evolutionary invariant, J. Mol. Evol. 6:1–14.
Hood, J. M., Fowler, A. V., and Zabin, I., 1978, On the evolution of ß-galactosidase, Proc. Natl. Acad. Sci. U.S.A. 75:113–116.
Hursh, D. A., Andrews, M. E., and Raff, R. A., 1987, A sea urchin gene encodes a polypeptide homologous to epidermal growth factor, Science 237:1487–1490.
Ichinose, A., McMullen, B. A., Fujikawa, K., and Davie, E. W., 1986, Amino acid sequence of the b subunit of human factor XIII, a protein composed of ten repetitive segments, Biochemistry 25:4633–4638.
Ivanov, O. C., and Ivanov, C. P., 1980, Some evidence for the universality of structural periodicity in proteins, J. Mol. Evol. 16:47–68.
Jackman, R. W., Beeler, D. L., VanDeWater, L., and Rosenberg, R. D., 1986, Characterization of a thrombomodulin cDNA reveals structural similarity to the low density lipoprotein receptor, Proc. Natl. Acad. Sci. U.S.A. 83:8834–8838.
Johnson, K. S., Taylor, D. W., and Cordingley, J. S., 1987, Possible eggshell protein gene from Schistosoma mansoni, Mol. Biochem. Parasitol. 22:89–100.
Jornvall, H., and Persson, B., 1983, Amino acid sequence restriction in relation to proteolysis, Biosci. Rep. 3: 225–232.
Jukes, T. H., 1966, Molecules and Evolution, Columbia University Press, New York.
Jukes, T. H., Holmquist, R., and Moise, H., 1975, Amino acid composition of proteins: Selection against the genetic code, Science 189:50–51.
Kabsch, W., and Sander, C., 1984, On the use of sequence homologies to predict protein structure: Identical pentapeptides can have completely different conformations, Proc. Natl. Acad. Sci. U.S.A. 81:1075–1078.
Kageyama, R., Ohkubo, H., and Nakanishi, S., 1984, Primary structure of human preangiotensinogen deduced from the cloned cDNA sequence, Biochemistry 23:3603–3609.
King, J. L., and Jukes, T. H., 1969, Non-Darwinian evolution, Science 164:788–798.
Kitamura, N., Semler, B. L., Rothberg, P. G., Larsen, G. R., Adler, C. J., Dorner, A. J., Emini, E. A., Hanecak, R., Lee, J. J., van der Werf, S., Anderson, W. W., and Wimmer, E., 1981, Primary structure, gene organization and polypeptide expression of poliovirus RNA, Nature 291:547–553.
Kobilka, B. K., Matsui, H., Kobilka, T. S., Yang-Feng, T. L., Francke, U., Caron, M. G., Lefkowitz, R. J., and Regan, J. W., 1987, Cloning, sequencing, and expression of the gene coding for the human platelet α2-adrenergic receptor, Science 238:650–656.
Krikos, A., Mutoh, N., Boyd, A., and Simon, M. I., 1983, Sensory transducers of E. coli are composed of discrete structural and functional domains, Cell 33:615–622.
Kristensen, T., and Tack, B. F., 1986, Murine protein H is comprised of 20 repeating units, 61 amino acids in length, Proc. Natl. Acad. Sci. U.S.A. 83:3963–3967.
Kubo, T., Fukuda, K., Mikami, A., Maeda, A., Takahashi, H., Mishina, M., Haga, T., Haga, K., Ichiyama, A., Kangawa, K., Kojima, M., Matsuo, H., Hirose, T., and Numa, S., 1986, Cloning, sequencing and expression of complementary DNA encoding the muscarinic acetylcholine receptor, Nature 323:411–416.
Kurachi, K., and Davie, E. W., 1982, Isolation and characterization of a cDNA coding for human factor IX, Proc. Natl. Acad. Sci. U.S.A. 79:6461–6464.
Laurent, B. C., Nilsson, M. H. L., Bavik, C. O., Jones, T. A., Sundelin, J., and Peterson, P. A., 1985, Characterization of the rat retinol-binding protein gene and comparison to the three-dimensional structure of the protein, J. Biol. Chem. 260: 11476–11480.
López Otin, C., Grubb, A. O., and Méndez, E., 1984, The complete amino acid sequence of human complex-forming glycoprotein heterogeneous in charge (protein HC) from one individual, Arch. Biochem. Biophys. 228:544–554.
Lozier, J., Takahashi, N., and Putnam, F. W., 1984, Complete amino acid sequence of human plasma ß2-glycoprotein I, Proc. Natl. Acad. Sci. U.S.A. 81:3640–3644.
Lundwall, A., Dackowski, W., Cohen, E., Shaffer, M., Mahr, A., Dahlback, B., Stenflo, J., and Wydro, R., 1986, Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation, Proc. Natl. Acad. Sci. U.S.A. 83:6716–6720.
Magnusson, R. P., Gestautas, J., Seto, P., Taurog, A., and Rapoport, B., 1986, Isolation and characterization of a cDNA clone for porcine thyroid peroxidase, FEBS Lett. 208:391–396.
Masu, Y., Nakayama, K., Tamaki, H., Harada, Y., Kuno, M., and Nakanishi, S., 1987, cDNA cloning of bovine substance-K receptor through oocyte expression system, Nature 329:836–838.
Mclachlan, A. D., 1977, Repeated helical pattern in apolipoprotein-A-I, Nature 267:465–466.
Mclachlan, A. D., Stewart, M., and Smillie, L. B., 1975, Sequence repeats in α-tropomyosin, J. Mol. Biol. 98:281–291.
McMullen, B. A., and Fujikawa, K., 1985, Amino acid sequence of the heavy chain of human α-factor XIIa (activated Hageman factor), J. Biol. Chem. 260:5328–5341.
McReynolds, L., O’Malley, B. W., Nisbet, A. D., Fothergill, J. E., Givol, D., Fields, S., Robertson, M., and Brownlee, G. G., 1978, Sequence of chicken ovalbumin mRNA, Nature 273:723–728.
Medof, M. E., Lublin, D. M., Holers, V. M., Ayers, D. J., Getty, R. R., Leykam, J. F., Atkinson, J. P., and Tykocinski, M. L., 1987, Cloning and characterization of cDNAs encoding the complete sequence of decay-accelerating factor of human complement, Proc. Natl. Acad. Sci. U.S.A. 84:2007–2011.
Mole, J. E., Anderson, J. K., Davison, E. A., and Woods, D. E., 1984, Complete primary structure for the zymogen of human complement factor B, J. Biol. Chem. 259:3407–3412.
Nagamine, Y., Pearson, D., Altus, M. S., and Reich, E., 1984, cDNA and gene nucleotide sequence of porcine plasminogen activator, Nucleic Acids Res. 12:9525–9541.
Netzker, R., Kchel, H. G., Basak, N., and Kntzel, H., 1982, Nucleotide sequence of Aspergillus nidulans mitochondrial genes coding for ATPase subunit 6, cytochrome oxidase subunit 3, seven unidentified proteins, four tRNAs and L-rRNA, Nucleic Acids Res. 10:4783–4794.
Ng, S. C., Rao, A. G., Zack Howard, O. M., and Sodetz, J. M., 1987, The eighth component of human complement: Evidence that it is an oligomeric serum protein assembled from products of three different genes, Biochemistry 26:5229–5233.
Ohno, S., 1984, Repeats of base oligomers as the primordial coding sequences of the primeval earth and their vestiges in modem genes, J. Mol. Evol. 20:313–321.
Pennica, D., Holmes, W. E., Kohr, W. J., Harkins, R. N., Vehar, G. A., Ward, C. A., Bennett, W. F., Yelverton, E., Seeburg, P. H., Heyneker, H. L., Goeddel, D. V., and Collen, D., 1983, Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli, Nature 301:214–221.
Pervaiz, S., and Brew, K., 1987, Homology and structure-function correlations between α1 acid glycoprotein and serum retinol-binding protein and its relatives, FASEB J. 1:209–214.
Poole, S. J., Kauvar, L. M., Drees, B., and Kornberg, T., 1985, The engrailed locus of drosophila: Structural analysis of an embryonic transcript, Cell 40:37–43.
Postle, K., and Good, R. F., 1983, DNA sequence of the Escherichia coli tonB gene, Proc. Natl. Acad. Sci. U.S.A. 80:5235–5239.
Putnam, F. W., Florent, G., Paul, C., Shinoda, T., and Shizizu, A., 1973, Complete amino acid sequence of the mu heavy chain of a human IgM immunoglobulin, Science 182:287–291.
Ragg, H., 1986, A new member of the plasma protease inhibitor gene family, Nucleic Acids Res. 14:1073–1088.
Ravetch, J. V., Feder, R., Pavlovec, A., and Blobel, G., 1984, Primary structure and genomic organization of the histidine-rich protein of the malaria parasite Plasmodium lophurae, Nature 312:616–620.
Reynolds, P., Prakash, L., Dumais, D., Perozzi, G., and Prakash, S., 1985, Nucleotide sequence of the RAD10 gene of Saccharomyces cerevisiae, EMBO J. 4:3549–3552.
Ricca, G. A., and Taylor, J. M., 1981, Nucleotide sequence of rat α-acid glycoprotein messenger RNA, J. Biol. Chem. 256:11199–11202.
Ruoslahti, E., and Pierschbacher, M. D., 1987, New perspectives in cell adhesion: RGD and integrins, Science 238:491–497.
Sai, S., Tanaka, T., Kosher, R. A., and Tanzer, M. L., 1986, Cloning and sequence analysis of a partial cDNA for chicken cartilage proteoglycan core protein, Proc. Natl. Acad. Sci. U.S.A. 83:5081–5085.
Saroff, H. A., and Pretorius, H. T., 1981, The uniqueness of protein sequences, Fed. Proc. 40:1676.
Scheller, R. H., Jackson, J. F., McAllister, L. B., Rothman, B. S., Mayeri, E., and Axel, R., 1983, A single gene encodes multiple neuropeptides mediating a stereotyped behavior, Cell 32:7–22.
Schmid, K., Kaufman, H., Isemura, S., Bauer, F., Emura, J., Motoyarma, T., Ishiguro, M., and Nanno, S., 1973, Structure of α1-acid glycoprotein. The complete amino acid sequence, multiple amino acid substitutions, and homology with the immunoglobulins, Biochemistry 12:2711–2724.
Schubert, D., LaCorbiere, M., and Esch, F., 1986, A chick neural retina adhesion and survival molecule is a retinol-binding protein, J. Cell Biol. 102:2295–2301.
Scott, J., Urdea, M., Quiroga, M., Sanchez-Pescador, R., Fong, N., Selby, M., Rutter, W. J., and Bell, G.I., 1983, Structure of a mouse submaxillary messenger RNA encoding epidermal growth factor and seven related proteins, Science 221:236–240.
Scott, R. A., Vanderkooi, G., Tuttle, R. W., Shames, P. M., and Scheraga, H. A., 1967, Minimization of polypeptide energy, III. Application of a rapid energy minimization technique to the calculation of preliminary structures of gramicidin-S, Proc. Natl. Acad. Sci. U.S.A. 58:2204–2211.
Sheumack, D. D., Claassens, R., Whiteley, N. M., and Howden, M. E. H., 1985, Complete amino acid sequence of a new type of lethal neurotoxin from the venom of the funnel-web spider Atrax robustus, FEBS Lett. 181:154–156.
Shimotohno, K., Takahashi, Y., Shimizu, N., Gojobori, T., Golde, D. W., Chen, I. S. Y., Miwa, M., and Sugimura, T., 1985, Complete nucleotide sequence of an infectious clone of human T-cell leukemia virus type II: An open reading frame for the protease gene, Proc. Natl. Acad. Sci. U.S.A. 82:3101–3105.
Sorm, F., 1959, Ahnlichkeitder struktur bei eiweißstoffen, in: 1st International Symposium on The Origin of Life (A. Oparin et al., eds.), Pergamon Press, Oxford, pp. 231–240.
Süahoff, T. C., Russell, D. W., Goldstein, J. L., Brown, M. S., Sanchez-Pescador, R., and Bell, G. I., 1985, Cassette of eight exons shared by genes for LDL receptor and EGF precursor, Science 228:893–895.
Sumi, Y., Nakamura, Y., Aoki, N., Sakai, M., and Muramatsu, M., 1986, Structure of the carboxyl-terminal half of human α2-plasmin inhibitor deduced from that of cDNA, J. Biochem. (Tokyo) 100:1399–1402.
Suzuki, K., Dehayashiki, Y., Nishioka, J., Kurachi, K., Akira, M., Yamamoto, S., and Hashimoto, S., 1987, Characterization of a cDNA for human protein C inhibitor, J. Biol. Chem. 262:611–615.
Van der Ploeg, L. H. T., 1987, Control of variant surface antigen switching in trypanosomes, Cell 51: 159–161.
Vehar, G. A., Keyt, B., Eaton, D., Rodriguez, H., O’Brien, D. P., Rotblat, F., Oppermann, H., Keck, R., Wood, W. I., Harkins, R. N., Tuddenham, E. G. D., Lawn, M., and Capon, D. J., 1984, Structure of human factor VIII, Nature 312:337–342.
Venkatesan, S., Gershowitz, A., and Moss, B., 1982, Complete nucleotide sequences of two adjacent early vaccinia virus genes located within the inverted terminal repetition, J. Viral. 44:637–646.
Wahlgren, M., Aslund, L., Fraźen, L., Sundvall, M., Wahlin, B., Berzins, K., McNicol, L. A., Björkman, A., Wigzell, H., Perlmann, P., and Pettersson, U., 1986, A Plasmodium falciparum antigen containing clusters of asparagine residues, Proc. Natl. Acad. Sci. U.S.A. 83:2677–2681.
Walker, J. E., Saraste, M., Runswick, M. J., and Gay, N. J., 1982, Distantly related sequences in the α-and ß-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold, EMBO J. 1:945–951.
Watson, D. C., and Dixon, G. H., 1981, Amino acid sequence homologies between the high-mobility-group proteins, HMB-T from trout testis and HMG-1 and-2 from calf thymus: Is the poly-aspartic-glutamic acid polypeptide within the main chain? Biosci. Reports 1:167–175.
Weiner, S., and Hood, L., 1975, Soluble protein of the organic matrix of mollusk shells: A potential template for shell formation, Science 190:987–989.
Wharton, K. A., Johansen, K. M., Xu, T., and Artavanis-Tsaknoas, S., 1985, Nucleotide sequence from the neurogenic locus notch implies a gene product that shares homology with proteins containing EGF-like repeats, Cell 43:567–581.
Wittmann-Liebold, B., Ashman, K., and Dzionara, M., 1983, Multiple internal repeats within protein S1 from the Escherichia coli ribosome, FEBS Lett. 154:31–41.
Yamamoto, T., Davis, C. G., Brown, M. S., Schneider, W. J., Casey, M. L., Goldstein, J. L., and Russell, D. W., 1984, The human LDL receptor: A cysteine-rich protein with multiple Alu sequences in its mRNA, Cell 39:27–38.
Ycas, M., 1972, De novo origin of periodic proteins, J. Mol. Evol. 2:17–27.
Zuckerkandl, E., 1975, The appearance of new structures and functions in proteins during evolution, J. Mol. Evol. 7: 1–57.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1989 Plenum Press, New York
About this chapter
Cite this chapter
Doolittle, R.F. (1989). Redundancies in Protein Sequences. In: Fasman, G.D. (eds) Prediction of Protein Structure and the Principles of Protein Conformation. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1571-1_14
Download citation
DOI: https://doi.org/10.1007/978-1-4613-1571-1_14
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4612-8860-2
Online ISBN: 978-1-4613-1571-1
eBook Packages: Springer Book Archive