Prediction of the Secondary Structure of Proteins From Their Amino Acid Sequence

Advances in Enzymology and Related Areas of Molecular Biology

Volumn 47, Issue , 2006, Pages 45-148

  Chou, Peter Y ^a   Fasman, Gerald D ^a  

^a BRANDEIS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE KINASE; GLUCAGON; HEMOGLOBIN S; LYSOZYME; OLIGOPEPTIDE; PROINSULIN; PROLINE; REPRESSOR PROTEIN; SUPEROXIDE DISMUTASE; TRYPSIN INHIBITOR;

AMINO ACID SEQUENCE; AUDIOVISUAL EQUIPMENT; HYDROGEN BOND; PROTEIN CONFORMATION; REVIEW;

ADENYLATE KINASE; AMINO ACID SEQUENCE; GLUCAGON; HEMOGLOBIN, SICKLE; HYDROGEN BONDING; MODELS, STRUCTURAL; MURAMIDASE; OLIGOPEPTIDES; PROINSULIN; PROLINE; PROTEIN CONFORMATION; REPRESSOR PROTEINS; SUPEROXIDE DISMUTASE; SUPPORT, U.S. GOV'T, NON-P.H.S.; SUPPORT, U.S. GOV'T, P.H.S.; TRYPSIN INHIBITORS;

EID: 0018110116     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470122921.ch2     Document Type: Chapter

References (267)

1. Liljas, A., and Rossmann, M. G., Ann. Rev. Biochem., 43, 475 (1974).
2. Matthews, B. W., in The Proteins, 3rd ed., H. Neurath and R. L. Hill, Eds., Academic Press, New York, 1975.
3. Anfinsen, C. B., Haber, E., Sela, M., and White, F. H., jr., Proc. Natl. Acad. Sci. U.S., 47, 1309 (1961).
4. Szent-Gyorgyi, A. G., and Cohen, C, Science, 126, 697 (1957).
5. Davies, D. R.J. Mol. Biol., 9, 605 (1964).
6. Blout, E. R., deLoze, C, Bloom, S. M., and Fasman, G. D.J. Amer. Chem. Soc, 82, 3787 (1960).
7. Blout, E. R., in Polyamino Acids, Polypeptides and Proteins, M. A. Stahmann, Ed., University of Wisconsin Press, Madison, 1962, p. 275.
8. Havsteen, B. H.J. Theor. Biol, 10, 1 (1966).
9. Goldsack, D. E., Biopolymers, 7, 299 (1969).
10. Scheraga, H. A.J. Amer. Chem. Soc, 82, 3847 (1960).
11. Kendrew.J. C, Dickerson, R. E., Strandberg, B. E., and Davies, D. R.,Nature, 185, 422 (1960).
12. Perutz, M. F., Rossman, M. G., Cullis, A. F., Muirhead. H., and North, A. C. T., Nature, 185, 416 (1960).
13. Edmundson, A. B., Nature, 205, 883 (1965).
14. Braunitzer, G., Hilse, K., Rudloff, V., and Hilschmann, N.,Adv. Protein Chem., 19, 1 (1964).
15. Guzzo, A. V., Biophys. J., 5, 809 (1965).
16. Prothero, J. W., Biophys. J., 6, 367 (1966).
17. Periti, P. F., Quagliarotti, G., and Liquori, A. M.J. Mol. Biol., 24, 313 (1967).
18. Low, B, W., Lovell, F. M., and Rudko, A. D., Proc. Natl. Acad. Sci. U.S., 60, 1519 (1968).
19. Kotelchuck, D., and Scheraga, H. A., Proc. Natl. Acad. Sci. U.S., 62, 14 (1969).
20. Schiffer, M., and Edmundson, A. B., Biophys. J., 7, 121 (1967).
21. Blundell, T., Dodson, G., Hodgkin, D., and Mercola, D., Adv. Protein Chem., 26, 279(1972).
22. Haggis, G. H., in Introduction to Molecular Biology, G. H. Haggis, Ed., Wiley, New York, 1964, p. 73.
23. Zimm, B. H., and Bragg, J. K.J. Chem. Phys., 31, 526 (1959).
24. Lewis, P. N., Go, N., Go, M., Kotelchuck, D., and Scheraga, H. A., Proc. Natl. Acad. Sci. U.S., 65, 810 (1970).
25. Lewis, P. N., and Scheraga, H. A., Arch. Biochem. Biophys., 144, 576 (1971).
26. Wu, T. T., and Kabat, E. A., Proc. Natl. Acad. Sci. U.S., 68, 1501 (1971).
27. Wu, T. T., and Kabat, E. A.J. Mol. Biol., 75, 13 (1973).
28. Robson, B., and Pain, R. H.J. Mol. Biol., 58, 237 (1971).
29. Finkelstein, A. V., and Ptitsyn, O. B.J. Mol. Biol., 62, 613 (1971).
30. Poland, D., and Scheraga, H. A., Theory of Helix-Coil Transitions in Biopolymers, Academic Press, New York, 1970.
31. Fasman, G. D., Ed., Poly-a-Amino Acids, Dekker, New York, 1967.
32. Richards, F. M., and Wyckoff, M. W., Enzymes, 3rd ed., 4, 647 (1971).
33. Birktoft, J. j., and Blow, D. M.J. Mol. Biol, 68, 187 (1972).
34. Shotton, D. M., and Watson, H. C., Nature, 225, 811 (1970).
35. Edelman, G. M., Cunningham, B. A., Reeke, G. N., Jr., Becker, J. W., Waxdal, M. J., and Wang, J. L., Proc. Natl. Acad. Sci. U.S., 69, 2580 (1972).
36. Ptitsyn, O. B., and Finkelstein, A. V., Biofizika, 15, 757 (1970).
37. Nagano, K.J. Mol. Biol, 75, 401 (1973).
38. Kabat, E. A., and Wu, T. T., Biopolymers, 12, 751 (1973).
39. Kabat, E. A., and Wu, T. T.,Proc. Natl. Acad. Sci. U.S., 70, 1473 (1973).
40. Chou, P. Y., Wells, M., and Fasman, G. D., Biochemistry, 11, 3028 (1972).
41. Chou, P. Y., and Fasman, G. D.J. Mol. Biol, 74, 263 (1973).
42. Chou, P. Y., and Fasman, G. D., Biochemistry, 13, 211 (1974).
43. Chou, P. Y., and Fasman, G. D., Biochemistry, 13, 222 (1974).
44. Quiocho, F. A., and Lipscomb, W. N.,Adv. Protein Chem., 25, 1 (1971).
45. Matthews, B. V/.,Biochim. Biophys. Acta, 405, 442 (1975).
46. Schulz, G. E., Elzinga, M., Marx, F., and Schirmer, R. H., Nature, 250, 120 (1974).
47. Liljas, A., Kannan, K. K., Bergsten, P-C, Waara, I., Fridborg, K., Strandberg, B., Carlbom, U., Jarup, L., Lovgren, S., and Petef, M., Nature New Biol, 235, 131 (1972).
48. Carter, C. W., Jr., Kraut, J., Freer, S. T., Xuong, Ng. H., Alden, R. A., and Bartsch, R. G.J. Biol. Chem., 249, 4212 (1974).
49. Salemme, F. R., Freer, S. T., Xuong, Ng. H., Alden, R. A., and Kraut, J.J. Biol. Chem., 248, 3910 (1973).
50. Adman, E. T., Sieker, L. C, and Jensen, L. H.J. Biol. Chem., 248, 3987 (1973).
51. Burnett, R. M., Darling, G. D., Kendall, D. S., LeQuesne, M. E., Mayhew, S. G., Smith, W. W., and Ludwig, M. L.J. Biol. Chem., 249, 4383 (1974).
52. Padlan, E. A., and Love, W. E.J. Biol. Chem., 249, 4067 (1974).
53. Huber, R., Epp, O., Steigemann, W., and Formanek, H.,Eur.J. Biochem., 19, 42 (1971).
54. Adams, M. J., Ford, G. C, Liljas, A., and Rossmann, M. G., Biochem. Biophys. Res. Commun., 53, 46 (1973).
55. Watenpaugh, K. D, Sieker, L. C, Herriott, J. R., and Jensen, L. H., Acta Crystallogr., B29, 943 (1973).
56. Herriott, J. R., Watenpaugh, K. D., Sieker, L. C, and Jensen, L. H.J. Mol. Biol, 80, 423 (1973).
57. IUPAC-IUB Commission on Biochemical Nomenclature, Biochemistry 9, 3471 (1970).
58. Pauling, L., Corey, R. B., and Branson, H. R., Proc. Natl. Acad. Sci. U.S., 37, 205 (1951).
59. Ramachandran, G. N., and Sasisekharan, V., Adv. Protein Chem., 23, 283 (1968).
60. Nemethy, G., Phillips, D. C., Leach, S. J., and Scheraga, H. A., Nature, 214, 363 (1967).
61. Lewis, P. N., Momany, F. A., and Scheraga, H. A., Proc. Natl. Acad. Sci. U.S., 68, 2293 (1971).
62. Kuntz, I. D.J. Amer. Chem. Soc, 94, 4009 (1972).
63. Crawford, J. L., Lipscomb, W. N., and Schellman, C. G., Proc Natl. Acad. Sci. U.S., 70, 538 (1973).
64. Lewis, P. N., Momany, F. A., and Scheraga, H. A.,Biochim. Biophys. Acta, 303, 211 (1973).
65. Venkatachalam, C. M., Biopolymers, 6, 1425 (1968).
66. Perlmann, G. E., and Katchalski, E.J. Amer. Chem. Soc, 84, 452 (1962).
67. Cook, D. A.J. Mol. Biol., 29, 167 (1967).
68. Ptitsyn, O. B.J. Mol. Biol., 42, 501 (1969).
69. Nozaki, Y., and Tanford, C.J. Biol. Chem., 246, 2211 (1971).
70. Aboderin, A. A., Int. J. Biochem., 2, 537 (1971).
71. Hardman, K. D., and Ainsworth, C. F., Biochemistry, 11, 4910 (1972).
72. McCubbin, W. D., Oikawa, K., and Kay, C. M., Biochem. Biophys. Res. Commun., 43, 666 (1971).
73. Visser, L., and Blout, E. R., Biochemistry, 10, 743 (1971).
74. Schiffer, M., and Edmundson, A. B., Biophys. J., 10, 293 (1970).
75. Low, B. W., Lovell, F. M., and Rudko, A. D., Biophys.]., 11, 235 (1971).
76. Chou, P. Y., and Fasman, G. D., Biochemistry, 14, 2536 (1975).
77. Srere, P. A., and Brooks, G. C.,Arch. Biochem. Biophys., 129, 708 (1969).
78. Chen, Y. H., Yang, J. T., and Martinez, H. M., Biochemistry, 11, 4120 (1972).
79. Gratzer, W. B., Bailey, E., and Beaven, G. H., Biochem. Biophys. Res. Commun., 28, 914 (1967).
80. Epand, R. M., Can.]. Biochem., 49, 166 (1971).
81. McBride-Warren, P. A., and Epand, R. M., Biochemistry, 11, 3571 (1972).
82. Panijpan, B., and Gratzer, W. B., Biochem., 45, 547 (1974).
83. Sasaki, K., Dockerill, S., Adamiak, D. A., Tickle, I. J., and Blundell, T., Nature, 257, 751 (1975).
84. Gilbert, W., and Muller-Hill, B., Proc. Natl. Acad. Sci. U.S., 56, 1891 (1966).
85. Miiller-Hill, B.,Angew. Chem. (Int. Ed.), 10, 160 (1971).
86. Gilbert, W., in Polymerization in Biological Systems, Vol. 7, Ciba Foundation Symposium, Associated Scientific Publishers, Amsterdam, 1972, p. 245.
87. Beyreuther, K., Adler, K., Geisler, N., and Klemm, A., Proc. Natl. Acad. Sci. U.S., 70, 3576 (1973).
88. Gilbert, W., and Maxam, A., Proc. Natl. Acad. Sci. U.S., 70, 3581 (1973).
89. Weber, K., Piatt, T., Ganem, D., and Miller, J. H.,Proc. Natl. Acad, Sci. U.S., 69, 3624 (1972).
90. Chou, P. Y., Adler, A. J., and Fasman, G. D.J. Mol. Biol., 96, 29 (1975).
91. Kendrew, j. C, Brookhaven Symp. Biol., 15, 216 (1962).
92. Carter, C. W., Jr., and Kraut, J., Proc. Natl. Acad. Sci. U.S., 71, 283 (1974).
93. Muller-Hill, B., Fanning, T., Geisler, N., Gho, D., Kania, J., Kathmann, P., Meissner, H., Schlotmann, M., Schmitz, A., Triesch, I., and Beyreuther, K., in Protein-Ligand Interactions, H. Sund and G. Blauer, Eds., de Gruyter, Berlin, 1975, p. 211.
94. Miller, J. H., Coulondre, C., Schmeissner, U., Schmitz, A., and Lu, P., in Protein-Ligand Interactions, H. Sund and G. Blauer, Eds., de Gruyter, Berlin, 1975, p. 238.
95. Bourgeois, S., and Pfahl, M.,Adv. Protein Chem., 30, 1 (1976).
96. Steitz, T. A., Richmond, T. J., Wise, D., and Engelman, D., Proc. Natl. Acad. Sci. V.S., 71, 593 (1974).
97. Ingram, V. U.,Biochim. Biophys. Acta, 36, 402'(1959).
98. Finch, J. T., Perutz, M. F., Bertles, J. F., and Dobler, J., Proc. Natl. Acad. Sci. U.S., 70, 718 (1973).
99. Edelstein, S. J., Telford, J. N., and Crepeau, R. H.,Proc. Natl. Acad. Sci. U.S., 70, 1104 (1973).
100. Hofrichter, J., Hendricker, D. G, and Eaton, W. A., Proc. Natl. Acad. Sci. U.S., 70, 3604 (1973).
101. Chou, P. Y., Biochem. Biophys. Res. Commun., 61, 87 (1974).
102. Murayama, M., Nature, 202, 258 (1964).
103. Perutz, M. F., Muirhead, H., Cox, J. M., Goaman, L. C. G., Nature, 219, 131 (1968).
104. Wishner, B. C, Ward, K. B., Lattman, E. E., and Love, W. E.J. Mol. Biol, 98, 179 (1975).
105. Ho, C, in Proceedings of the Symposium on Molecular and Cellular Aspects of Sickle Cell Disease, J. I. Hercules, G. L. Cottam, M. R. Waterman, and A. N. Schech-ter, Eds., U. S. Government Printing Office, 1976, pp. 65-85.
106. Curr. Contents, 19, No. 8, 5 (1976).
107. Wootton, J. C, Nature, 252, 542 (1974).
108. Anderson, R. A., Nakashima, Y., and Coleman, J. E., Biochemistry, 14, 907 (1975).
109. Snell, C. R., and Smyth, D. G.J. Biol. Chem., 250, 6291 (1975).
110. Durham, A. C. H., and Butler, P.J. G., Eur. J. Biochem., 53, 397 (1975).
111. Parry, D. A. D.J. Mol. Biol, 98, 519 (1975).
112. Stadler, H., FEBS Lett., 48, 114 (1974).
113. Chen, R., and Wittman-Liebold, B., FEBS Lett, 52, 139 (1975).
114. Hitz, H., Schafer, D., and Wittmann-Liebold, B., FEBS Lett., 56, 259 (1975) .
115. Brosius, J., Schiltz, E., and Chen, R., FEBS Lett., 56, 359 (1975).
116. Chen, R., Mende, L., Arfsten, U., FEBS Lett, 59, 96 (1975).
117. Yaguchi, U., FEBS Lett., 59, 217 (1975).
118. Ritter, E., and Wittmann-Liebold, B., FEBS Lett, 60, 153 (1975).
119. Bitar, K. G., and Wittmann-Liebold, B., Hoppe-Seyler's Z. Physiol. Chem., 356, 1343 (1975).
120. Vandekerckhove, J., Rombauts, W., Peeters, B., and Wittmann-Liebold, B., Hoppe-Seyler's 1. Physiol. Chem., 356, 1955 (1975).
121. Stadler, H., and Wittmann-Liebold, B., Eur. J. Biochem., 66, 49 (1976).
122. Wittmann-Liebold, B., Marzinzig, E., and Lehmann, A., FEBS Lett., 68, 110 (1976) .
123. Wittmann-Liebold, B., and Pannenbecker, K., FEBS Lett., 68, 115 (1976).
124. Morinaga, T., Funatsu, G., Funatsu, M., and Wittmann, H. G., FEBS Lett, 64, 307 (1976).
125. Chen, R., and Ehrke, G., FEBS Lett., 69, 240 (1976).
126. Dunn, B. M., and Chaiken, I. M.J. Mol. Biol, 95, 497 (1975).
127. Wood, H. G., and Zwolinski, G. K., Crit. Rev. Biochem., 4, 47 (1976).
128. Holladay, L. A., and Puett, D.,Proc. Natl. Acad. Sci. U.S., 73, 1199 (1976).
129. Holladay, L. A., Savage, C. R., Jr., Cohen, S., and Puett, D., Biochemistry, 15, 2624 (1976).
130. Klotz, I. M., Klippenstein, G. L., and Hendrickson, W. A., Science, 192, 335 (1976).
131. Aubert, J. P., and Loucheux-Lefebvre, M. H., Arch, Biochem. Biophys., 175, 400(1976).
132. Aubert, J. P., Biserte, G., and Loucheux-Lefebvre, M. H., Arch. Biochem. Biophys., 175, 410 (1976).
133. Wallace, D. G., Biophys. Chem., 4, 123 (1976).
134. Munoz, P. A., Warren, J. R., and Noelken, M. E., Biochemistry, 15, 4666(1976).
135. Brett, M., Chambers, G. K., Holder, A. A., Fincham, J. R. S., and Wootton, J. C.J. Mol Biol, 106, 1 (1976).
136. Stellwagen, E.J. Mol. Biol, 106, 903 (1976).
137. Banner, D. W., Bloomer, A. C, Petsko, G. A., Phillips, D. C, Pogson, C. I., Wilson, I. A., Corran, P. H., Furth, A. J., Milman, J. D., Offord, R. E., Priddle, J. D., and Waley, S. G., Nature, 255, 609 (1975).
138. Nozaki, Y., Chamberlain, B. K., Webster, R. E., and Tanford, C, Nature, 259, 335 (1976).
139. Low, B. W., Preston, H. S., Sato, A., Rosen, L. S., Searl, J. E., Rudko, A. D., and Richardson, J. S., Proc. Natl Acad. Sci. U.S., 73, 2991 (1976).
140. Krigbaum, W. R., and Knutton, S. P., Proc. Natl. Acad. Sci. U.S., 70, 2809 (1973).
141. Froimowitz, M., and Fasman, G. D., Macromolecules, 7, 583 (1974).
142. Blagdon, D. E., and Goodman, M., Biopolymers, 14, 241 (1975).
143. Periti, P., Estratto Boll. Chim. Farm., 113, 187 (1974).
144. Burgess, A. W., Ponnuswamy, P. K., and Scheraga, H. A., Isr. J. Chem., 12, 239 (1974).
145. Robson, B., Biochem. J., 141, 853 (1974).
146. Robson, B., and Pain, R. H., Biochem. J., 141, 869 (1974).
147. Robson, B., and Pain, R. H., Biochem. J., 141, 883 (1974).
148. Robson, B., and Pain, R. H., Biochem. J., 141, 899 (1974).
149. Robson, B., and Pain, R. H., Nature New Biol, 238, 107 (1972).
150. Burgess, A. W., and Scheraga, H. A., Proc. Natl Acad. Sci. U.S., 72, 1221 (1975).
151. Nagano, K.J. Mol. Biol, 84, 337 (1974).
152. Nagano, K., and Hasegawa, K.J. Mol. Biol, 94, 257 (1975).
153. Levitt, M.J. Mol. Biol, 82, 393 (1974).
154. Warme, P. K., and Scheraga, H. A., Biochemistry, 13, 757 (1974).
155. Patau, J., and Puigdomenech, P.J. Mol. Biol, 88, 457 (1974).
156. Lim, V. I.J. Mol. Biol, 88, 857 (1974).
157. Lim, V. I.J. Mol. Biol, 88, 873 (1974).
158. Finkelstein, A. V., and Ptitsyn, O. B.J. Mol. Biol, 103, 15 (1976).
159. Schulz, G. E., Barry, C. D., Friedman, J., Chou, P. Y., Fasman, G. D., Finkelstein, A. V., Lim, V. I., Ptitsyn, O. B., Kabat, E. A., Wu, T. T., Levitt, M., Robson, B., and Nagano, K., Nature, 250, 140 (1974).
160. Kabat, E. A., and Wu, T. T.,Proc. Natl. Acad. Sci. U.S., 71, 4217 (1974).
161. Matthews, B. W., and Remington, S. J., Proc. Natl. Acad. Sci. U.S., 71, 4178 (1974).
162. Leberman, R.J. Mol. Biol, 55, 28 (1971).
163. Schellman, C. G., Chemical Rubber Company Crit. Rev. Biochem., to be published.
164. Tanaka, S., and Scheraga, H. A., Macromolecules, 9, 168 (1976).
165. Huber, R., Kukla, D., Riihlmann, A., and Steigemann, W., Cold Spring Harbor Symp. Quant. Biol, 36, 141 (1972).
166. Deisenhofer, J., and Steigemann, VJ.,Acta Crystallogr., B31, 238 (1975).
167. Holmgren, A., Soderberg, B. C, Eklund, H., and Branden, C. I., Proc. Natl. Acad. Sci. U.S., 72, 2305 (1975).
168. Holmgren, A., Eur. J. Biochem., 6, 475 (1968).
169. Hendrickson, W. A., and Ward, K. B., Biochem. Biophys. Res. Commun., 66, 1349 (1975).
170. Richardson, J. S., Thomas, K. A., and Richardson, D. C, Biochem. Biophys. Res. Commun., 63, 986 (1975).
171. Laskowski, M., Jr., Kato, I., Leary, T. R., Schrode, J., and Sealock, R. W., Bayer-Symp. V Proteinase Inhibitors, H. Fritz, H. Tschesche, L.J. Greene, and E. Truscheit, Eds., Springer-Verlag, Berlin, 1974, p. 597.
172. Creighton, T. E., Nature, 255, 743 (1975).
173. Reddy, M. N., Keim, P. S., Heinrikson, R. L., and Kezdy, F.J. Biol. Chem., 250, 1741 (1975).
174. Creighton, T. E.J. Mol. Biol, 95, 107 (1975).
175. Creighton, T. E.J. Mol Biol, 96, 767 (1975).
176. Riihlmann, A., Kukla, D., Schwager, P., Bartels, K., and Huber, R.J. Mol. Bwl, 77, 417 (1973).
177. Lewis, P. N., and Bradbury, E. M., Biochim. Biophys. Acta, 336, 153 (1974).
178. Maxfield, F. R., and Scheraga, H. A., Macromolecules, 8, 491 (1975).
179. Vorob'ev, V. I., Birshtein, T. M., Aleksanyan, V. I., and Zalenskii, A. 0.,Mol. Biol, 6, 346 (1972).
180. Fasman, G. D., Chou, P. Y., and Adler, A. D., Biophys.]., 16, 1201 (1976).
181. Argos, P., Schwarz, J., and Schwarz, J.,Biochim. Biophys. Acta, 439, 261 (1976).
182. Kretsinger, R. H., and Barry, C. D., Biochim. Biophys. Acta, 405, 40 (1975).
183. Wetlaufer, D. B.,Proc. Natl. Acad. Sci. U.S., 70, 697 (1973).
184. Ramachandran, G. N., Ramakrishnan, C, and Sasisekharan, V.J. Mol. Biol, 7, 95 (1963).
185. Phillips, D. C, in British Biochemistry, Past and Present, T. W. Goodwin, Ed., Academic Press, London, 1970, p. 11.
186. Nishikawa, K., and Ooi, T.J. Phys. Soc. Jap., 32, 1338 (1972)
187. Ooi, T., and Nishikawa, K., in Conformation of Biological Molecules and Polymers, E. D. Bergmann and B. Pullman, Eds., Academic Press, New York, 1973, p. 173.
188. Rossmann, M. G., and Liljas, A.J. Mol. Biol, 85, 177 (1974).
189. Rossmann, M. G., Moras, D., and Olsen, K. W., Nature, 250, 194 (1974).
190. Rossmann, M. G., and Argos, P.J. Biol. Chem., 250, 7525 (1975).
191. Richardson, J. S., Richardson, D. C., Thomas, K. A., Silverton, E. W., and Davies, D. R.J. Mol. Biol., 102, 221 (1976).
192. Levitt, M., and Chothia, C, Nature, 261, 552 (1976).
193. Dunn, J. B., and Klotz, I. M.,Arch. Biochem. Biophys., 167, 615 (1975).
194. Kuntz, I. D.J. Amer. Chem. Soc, 97, 4362 (1975).
195. Richardson, J. S., Proc. Natl. Acad, Sci. U.S., 73, 2619 (1976).
196. Sternberg, M.J. E., and Thorton, J. M.J. Mol. Biol., 105, 367 (1976).
197. Ralston, E., and DeCoen, J. L.J. Mol. Biol., 83, 393 (1974).
198. Tanaka, S., and Scheraga, H. A., Proc Natl. Acad. Sci. U.S., 72, 3802 (1975).
199. Ptitsyn, O. B., and Rashin, A. A., Biophys. Chem., 3, 1 (1975).
200. Levitt, M., and Warshel, A., Nature, 253, 694 (1975).
201. Warshel, A., and Levitt, M.J. Mol. Biol., 106, 421 (1976).
202. Karplus, M., and Weaver, D. L., Nature, 260, 404 (1976).
203. De Haen, C, Swanson, E., and Teller, D. C., Biopolymers, 15, 1825 (1976).
204. Kuntz, I. D., Crippen, G. M., Kollman, P. A., and Kimelman, D.J. Mol. Biol., 106, 983 (1976).
205. Wu, T. T., Fitch, W. M., and Margoliash, E., Ann. Rev. Biochem., 43, 539 (1974).
206. Anfinsen, C. B., and Scheraga, H. A., Adv. Protein Chem., 29, 205 (1975).
207. Srinivasan, R., Balasubramanian, R., and Rajan, S. S., Science, 194, 720 (1976).
208. Schmid, K., Chen, L. C. H., Occhino, J. C, Foster, J. A., and Sperandio, K., Biochemistry, 15, 2245 (1976).
209. Low, M., Kisfaludy, L., and Fermandjian, S., Acta Biochim. Biophys. Acta Sci. Hung., 10, 229 (1975).
210. Greff, D., Toma, F., Fermandjian, S., Low, M., and Kisfaludy, L., Biochim. Biophys. Acta, 439, 219 (1976).
211. Li, L. K., and Spector, A., Exp. Eye Res., 19, 49 (1974).
212. Scanu, A. M., Edelstein, C, and Keim, P., in The Plasma Proteins, 2nd ed., Vol. I, Academic Press, New York, 1975, p. 317.
213. Andrews, A. L., Atkinson, D., Barratt, M. D., Finer, E. G., Hauser, H., Henry, R., Leslie, R. B., Owens, N. L., Phillips, M. C, and Robertson, R. N., Eur. J. Biochem., 64, 549 (1976).
214. Stoffel, W., and Darr, W., Hoppe-Seyler's Z. Physiol. Chem., 357, 127 (1976).
215. Edelstein, C, Noyes, C, Keim, P., Heinrikson, R. L., Fellows, R. E., and Scanu, A. M., Biochemistry, 15, 1262 (1976).
216. Green, N. U.,Adv. Protein Chem., 29, 102 (1975).
217. Nakashima, Y., Wiseman, R. L., Konigsberg, W., Marvin, D. A., Nature, 253, 68 (1975).
218. Green, N. M., and Flanagan, M. T., Biochem. J., 153, 729 (1976).
219. Thomas, G. J., Jr., Prescott, B., McDonald-Ordzie, P. E., and Hartman, K. A.J. Mol. Biol, 102, 103 (1976).
220. Isobe, T., Black, L. W., and Tsugita, A.J. Mol. Biol, 102, 349 (1976).
221. Gleisner, J. M., Peterson, D. L., and Blakley, R. L., Proc. Natl. Acad, Sci. U.S., 71, 3001 (1974).
222. Peterson, D. L., Gleisner, J. M., and Blakley, R. L.J. Biol. Chem., 250, 4945 (1975).
223. Tanaka, M., Haniu, M., Yasunobu, K. T., Biochem. Biophys. Res. Commun., 66, 639 (1975).
224. Olsen, K. W., Moras, D., Rossmann, M. G., and Harris, J. I.J. Biol. Chem., 250, 9313 (1975).
225. Yang, J. T.,Bwchem. Biophys. Res. Commun., 63, 232 (1975).
226. Smythies, J. R., Benington, F., Bradley, R. J., Morin, R. D., and Romine, W. O., Jr. J. Theor. Biol., 47, 309 (1974).
227. Bradbury, E. M., Cary, P. D., Crane-Robinson, C, Rattle, H. W. E., Boublik, M., and Sautiere, P., Biochemistry, 14, 1876 (1975).
228. Garel, A., Kovacs, A. M., Champagne, M., and Daune, M., Biochim. Biophys. Acta, 395, 5 (1975).
229. Lewis, P. N., Bradbury, E. M., and Crane-Robinson, C, Biochemistry, 14, 3391 (1975).
230. Pekary, A. E., Chan, S. I., Hsu, C. J., and Wagner, T. E., Biochemistry, 14, 1184 (1975).
231. Kawauchi, H., and Li, C. H.,Arch. Biochem. Biophys., 165, 255 (1974).
232. Peiia, C, Stewart, J. M., Paladini, A. C, Dellacha, J. M., and Santome, J. A., in Peptides: Chemistry, Structure, and Biology, R. Walter and J. Meienhofer, Eds., Ann Arbor Science Publishers, Ann Arbor, 1975, p. 523.
233. Low, T. L. K., Liu, Y. S. V., and Putnam, F. W., Science, 191, 390 (1976).
234. Moroder, L., Filippi, B., Borin, G., and Marchiori, F., Biopolymers, 14, 2075 (1975).
235. Looze, Y., Polastro, E., Gielens, C, and Leonis, ].,Biochem J., 157, 773 (1976).
236. Mavridis, I. M., and Tulinsky, A., Biochemistry, 15, 4410 (1976).
237. Patel, D. J., Biochemistry, 14, 1057 (1975).
238. Bradbury, A. F., Smyth, D. G., and Snell, C. R.,Biochem. Biophys. Res. Commun., 69, 950 (1976).
239. Gamier, J., Pernollet, J. C, Tertrin-Clary, C, Salesse, R., Casteing, M., Bar-navon, M., de la Llosa, and Jutisz, M., Eur. J. Biochem., 53, 243 (1975).
240. Bradbury, A. F., Smyth, D. G., and Snell, C. R., Nature, 260, 165 (1976).
241. Maeda, H., Glaser, C. B., Kuromizu, K., and Meienhofer, J., Arch. Biochem. Biophys., 164, 379 (1974).
242. Argos, P., Biochem. Biophys. Res. Commun., 70, 805 (1976).
243. Tsetlin, V. I., Mikhaleva, I. I., Myagkova, M. A., Senyavina, L. B., Arseniev, A. S., Ivanov, V. T., and Ovchinnikov, Y. A., in Peptides: Chemistry, Structure, and Biology, R. Walter and J. Meienhofer, Eds., Ann Arbor Science Publishers, Ann Arbor, 1975, p. 935.
244. Smythies, J. R., Benington, F., Bradley, R. J., Bridges, W. F., Morin, R. D., and Romine, W. O., Jr. J. Theor. Biol., 51, 111 (1975).
245. Cohn, D. V., and Hamilton, J. W., personal communication.
246. Vogt, H. P., Wollmer, A., Naithani, V. K., and Zahn, H., Hoppe-Seyler's Z. Physiol. Chem., 357, 107 (1976).
247. Lenstra, J. A., Hofsteenge, J., and Beintema, J. J., Abstracts, 10th International Congress of Biochemistry, Hamburg, Germany, 1976, p. 216.
248. Vassos, A., Higo, K. I., and Marcus, L., Biochim. Biophys. Acta, 427, 371 (1976).
249. Fink, M. L., and Bodanszky, M.J. Amer. Chem. Soc, 98, 974 (1976).
250. Bodanszky, M., and Fink, M. L., Bioorg. Chem., 5, 275 (1976).
251. Rivier, J., Brown, M., and Vale, W., Biochem. Biophys. Res. Commun., 65, 746 (1975) .
252. Tai,J. Y., Kortt, A. A., Liu, T. Y., and Elliott, S. D.J. Biol. Chem., 251, 1955 (1976) .
253. Reed, R. G., Feldhoff, R. C., Clute, O. L., and Peters, T'.Jr., Biochemistry, 14, 4578 (1975).
254. Zurawski, V. R., Jr., Kohr, W. J., and Foster, J. F., Biochemistry, 14, 5579 (1975).
255. Wunderer, G., Fritz, H., Wachter, E., and Machleidt, W.,J. Biochem., 68, 193 (1976).
256. Turano, T. A., Hartman, K. A., and Thomas, G. J., Jr. J. Phys. Chem., 80, 1157 (1976).
257. Mathews, F. S., Levine, M., and Argos, P.J. Mol. Biol., 64, 449 (1972).
258. Mathews, F. S., Argos, P., and Levine, M., Cold Spring Harbor Symp. Quant. Biol., 36, 387 (1972).
259. Dickerson, R. E., Takano, T., Eisenberg, D., Kallai, O. B., Samson, L., Cooper, A., and Margoliash, E.J. Biol. Chem., 246, 1511 (1971).
260. Takano, T., Kallai, O. B., Swanson, R., and Dickerson, R. E.J. Biol. Chem., 248, 5234 (1973).
261. Bendey, G., Dodson, E., Dodson, G., Hodgkin, D., and Mercola, D., Nature, 261, 166 (1976).
262. Deber, C. M., Madison, V., and Blout, E. R.,Acc. Chem. Res., 9, 106 (1976).
263. Kopple, K. D., Go, A., and Pilipauskas, D. R.J. Amer. Chem. Soc, 97, 6830 (1975).
264. Kopple, K. D., and Go, A., in Peptides: Chemistry, Structure and Biology, R. Walter and J. Meienhofer, Eds., Ann Arbor Science Publishers, Ann Arbor, 1975, p. 139.
265. Protein Data Bank, Brookhaven National Laboratories, Upton, New York, T. F. Koetzle, personal communication.
266. Chou, P. Y. and Fasman, G. D.J. Mol. Biol, 115, 135 (1977).
267. Remington, S. J., Anderson, W. F., Owen, J., Ten Eyck, L. F., Grainger, C. T., and Matthews, B. W.J. Mol. Biol. 118, 81 (1978).