The application of circular dichroism to studies of protein folding and unfolding
10.1016/s0167-4838(96)00190-2
Crossref journal-article
Elsevier BV
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology (78)
Bibliography

Kelly, S. M., & Price, N. C. (1997). The application of circular dichroism to studies of protein folding and unfolding. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1338(2), 161–185.

Authors 2
  1. Sharon M Kelly (first)
  2. Nicholas C Price (additional)
References 118 Referenced 419
  1. Adler, A.J., Greenfield, N.J. and Fasman, G.D. (1973) Methods Enzymol. 27, 675–735. (10.1016/S0076-6879(73)27030-1)
  2. Woody, R.W. (1995) Methods Enzymol. 246, 34–71. (10.1016/0076-6879(95)46006-3)
  3. Fasman, G.D. (ed.) (1996) Circular Dichroism and the Conformational Analysis of Biomolecules 738 pp., Plenum Press, New York. (10.1007/978-1-4757-2508-7)
  4. Jaenicke, R. (1987) Prog. Biophys. Mol. Biol. 49, 117–237. (10.1016/0079-6107(87)90011-3)
  5. Jaenicke, R. (1991) Biochemistry 30, 3147–3161. (10.1021/bi00227a001)
  6. Gething, M.-J. and Sambrook, J. (1992) Nature 355, 33–44. (10.1038/355033a0)
  7. Hlodan, R. and Hartl, F.U. (1994) in Mechanisms of Protein Folding (Pain, R.H., ed.), pp. 194–228, Oxford University Press, Oxford. (10.1093/oso/9780199633968.003.0008)
  8. Hartl, F.U. (1996) Nature 381, 571–580. (10.1038/381571a0)
  9. Marston, F.A.O. (1986) Biochem. J. 240, 1–12. (10.1042/bj2400001)
  10. Thatcher, D.R. and Hitchcock, A. (1994) in Mechanisms of Protein Folding (Pain, R.H., ed.), pp. 229–261, Oxford University Press, Oxford. (10.1093/oso/9780199633968.003.0009)
  11. Ramage, R., Green, J., Muir, T.W., Ogunjobi, O.M., Love, S. and Shaw, K. (1994) Biochem. J. 299, 151–158. (10.1042/bj2990151)
  12. Thomas, P.J., Qu, B.-H. and Pedersen, P.L. (1995) Trends Biochem. Sci. 20, 456–459. (10.1016/S0968-0004(00)89100-8)
  13. Sifers, R.N. (1995) Struct. Biol. 2, 355–357. (10.1038/nsb0595-355)
  14. Pace, C.N. (1990) Trends Biotechnol. 8, 93–98. (10.1016/0167-7799(90)90146-O)
  15. Kosen, P.A., Creighton, T.E. and Blout, E.R. (1981) Biochemistry 20, 5744–5760. (10.1021/bi00523a017)
  16. Takagi, T. and Ito, N. (1972) Biochim. Biophys. Acta 257, 1–10. (10.1016/0005-2795(72)90247-4)
  17. Chaffotte, A.F., Guillou, Y. and Goldberg, M.E. (1992) Biochemistry 31, 9694–9702. (10.1021/bi00155a024)
  18. Woody, R.W. (1994) Eur. Biophys. J. 23, 253–262. (10.1007/BF00213575)
  19. Freskgård, P.-O., Mårtensson, L.-G., Jonasson, P., Jonsson, B.-H. and Carlsson, U. (1994) Biochemistry 33, 14281–14288. (10.1021/bi00251a041)
  20. Hirst, J.D. and Brooks, C.L.,III (1994) J. Mol. Biol. 243, 173–178. (10.1006/jmbi.1994.1644)
  21. Provencher, S.W. and Glöckner, J. (1981) Biochemistry 20, 33–37. (10.1021/bi00504a006)
  22. Manavalan, P. and Johnson, W.C., Jr. (1987) Anal. Biochem. 167, 76–85. (10.1016/0003-2697(87)90135-7)
  23. Johnson, W.C., Jr. (1990) Proteins Struct. Funct. Genet. 7, 205–214. (10.1002/prot.340070302)
  24. Sutherland, J.C. (1996) in Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G.D., ed.), pp. 599–633, Plenum Press, New York. (10.1007/978-1-4757-2508-7_17)
  25. Barrow, C.J., Yasuda, A., Kenny, P.T.M. and Zagorski, M.G. (1992) J. Mol. Biol. 225, 1075–1093. (10.1016/0022-2836(92)90106-T)
  26. Yang, J.T., Wu, C.-S.C. and Martinez, H.M. (1986) Methods Enzymol. 130, 208–269. (10.1016/0076-6879(86)30013-2)
  27. Greenfield, N.J. (1996) Anal. Biochem. 235, 1–10. (10.1006/abio.1996.0084)
  28. Venyaminov, S.Yu. and Yang, J.T. (1996) in Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G.D., ed.), pp. 69–107, Plenum Press, New York. (10.1007/978-1-4757-2508-7_3)
  29. Strickland, E.H. (1974) Crit. Rev. Biochem. 2, 113–175. (10.3109/10409237409105445)
  30. Kahn, P.C. (1979) Methods Enzymol. 61, 339–378. (10.1016/0076-6879(79)61018-2)
  31. Woody, R.W. and Dunker, A.K. (1996) in Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G.D., ed.), pp. 109–157, Plenum Press, New York. (10.1007/978-1-4757-2508-7_4)
  32. Griffin, J.H., Rosenbusch, J.P., Weber, K.K. and Blout, E.R. (1972) J. Biol. Chem. 247, 6482–6490.
  33. Craig, S., Pain, R.H., Schmeissner, U., Virden, R. and Wingfield, T.P. (1989) Int. J. Pept. Protein Res. 33, 256–262. (10.1111/j.1399-3011.1989.tb01279.x)
  34. Coleman, J.E. (1968) J. Biol. Chem. 243, 4574–4587.
  35. Price, N.C. and Stevens, E. (1983) Biochem. J. 213, 595–602. (10.1042/bj2130595)
  36. Andersson, L.A. and Peterson, J.A. (1995) Biochem. Biophys. Res. Commun. 211, 389–395. (10.1006/bbrc.1995.1826)
  37. Munro, A.W, Lindsay, J.G., Coggins, J.R., Kelly, S.M. and Price, N.C. (1994) FEBS Lett. 343, 70–74. (10.1016/0014-5793(94)80609-8)
  38. Cogdell, R.J. and Scheer, H. (1985) Photochem. Photobiol. 42, 669–689. (10.1111/j.1751-1097.1985.tb01629.x)
  39. McDermott, G., Prince, S.M., Freer, A.A., Hawthornethwaite-Lawless, A.M., Papiz, M.Z., Cogdell, R.J. and Isaacs, N.W. (1995) Nature 374, 517–521. (10.1038/374517a0)
  40. Martin, S.R. (1996) in Proteins Labfax (Price, N.C., ed.), pp. 195–204, Bios Scientific Publishers, Oxford.
  41. Johnson, W.C., Jr. (1996) in Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G.D., ed.), pp. 635–652, Plenum Press, New York. (10.1007/978-1-4757-2508-7_18)
  42. Price, N.C. (1996) in Enzymology Labfax (Engel, P.C., ed.), pp. 34–41, Bios Scientific Publishers, Oxford.
  43. McRee, D.E. (1993) Practical Protein Crystallography, Academic Press, London. (10.1016/B978-0-12-486050-6.50008-5)
  44. Drenth, J. (1994) Principles of Protein Crystallography, Springer, Berlin. (10.1007/978-1-4757-2335-9)
  45. James, T.L. and Oppenheimer, N.J. (eds.) (1994) Nuclear Magnetic Resonance Part C, Methods Enzymol. Vol 239, 813 pp., Academic Press, San Diego, CA.
  46. Whitehead, B. and Waltho, J.P. (1996) in Proteins Labfax (Price, N.C., ed.), pp. 205–216, Bios Scientific Publishers, Oxford.
  47. Weiss, M.A., Ellenberger, T., Wobbe, C.R., Lee, J.P., Harrsion, S.C. and Struhl, K. (1990) Nature 347, 575–578. (10.1038/347575a0)
  48. Luchins, J. and Beychok, S. (1978) Science 199, 425–426. (10.1126/science.619462)
  49. Pflumm, M., Luchins, J. and Beychok, S. (1986) Methods Enzymol. 130, 519–534. (10.1016/0076-6879(86)30024-7)
  50. Kuwajima, K. (1996) in Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G.D., ed.). pp. 159–182, Plenum Press, New York. (10.1007/978-1-4757-2508-7_5)
  51. Ribas de Pouplan, L, Atrian, S., Gonzalez-Duarte, R., Fothergill-Gilmore, L.A., Kelly, S.M. and Price, N.C. (1991) Biochem. J. 276, 433–438. (10.1042/bj2760433)
  52. Robertson, A.G.S. and Nimmo, H.G. (1995) Biochem. J. 305, 239–244. (10.1042/bj3050239)
  53. Krell, T., Horsburgh, M.J., Cooper, A., Kelly, S.M. and Coggins, J.R. (1996) J. Biol. Chem. 271, 24492–24497. (10.1074/jbc.271.40.24492)
  54. Gilletto, A. and Pace, C.N. (1996) in Proteins Labfax (Price, N.C., ed.), pp. 233–239, Bios Scientific Publishers, Oxford.
  55. Moore, J.D., Hawkins, A.R., Charles, I.G., Deka, R., Coggins, J.R., Cooper, A., Kelly, S.M. and Price, N.C. (1993) Biochem. J. 295, 277–285. (10.1042/bj2950277)
  56. Pace, C.N. (1986) Methods Enzymol. 131, 266–280. (10.1016/0076-6879(86)31045-0)
  57. Wong, K.-P. and Tanford, C. (1973) J. Biol. Chem. 248, 8518–8523.
  58. Matthews, C.R. and Crisanti, M.M. (1981) Biochemistry 20, 784–792. (10.1021/bi00507a021)
  59. Ogasahara, K. and Yutani, K. (1994) J. Mol. Biol. 236, 1227–1240. (10.1016/0022-2836(94)90023-X)
  60. Tanford, C. (1970) Adv. Protein Chem. 24, 1–95. (10.1016/S0065-3233(08)60241-7)
  61. Johnson, C.M. and Fersht, A.R. (1995) Biochemistry 34, 6795–6804. (10.1021/bi00020a026)
  62. Scholtz, J.M., Barrick, D., York, E.J., Stewart, J.M. and Baldwin, R.L. (1995) Proc. Natl. Acad. Sci. USA 92, 185–189. (10.1073/pnas.92.1.185)
  63. Kuwajima, K., Nitta, K., Yoneyama, M. and Sugai, S. (1976) J. Mol. Biol. 106, 359–373. (10.1016/0022-2836(76)90091-7)
  64. Dolgikh, D.A., Gilmanshin, R.I., Brazhnikov, E.V., Bychkova, V.E., Semisotnov, G.V., Venyanimov, S.Yu. and Ptitsyn, O.B. (1981) FEBS Lett. 136, 311–315. (10.1016/0014-5793(81)80642-4)
  65. Christensen, H. and Pain, R.H. (1991) Eur. J. Biophys. 19, 221–229. (10.1007/BF00183530)
  66. Christensen, H. and Pain, R.H. (1994) in Mechanisms of Protein Folding (Pain, R.H., ed.), pp. 55–79, Oxford University Press, Oxford. (10.1093/oso/9780199633968.003.0003)
  67. Dobson, C.M. (1992) Curr. Opin. Struct. Biol. 2, 6–12. (10.1016/0959-440X(92)90169-8)
  68. Ptitsyn, O.B. (1995) Curr. Opin. Struct. Biol. 5, 74–78. (10.1016/0959-440X(95)80011-O)
  69. Jennings, P.A. and Wright, P.E. (1993) Science 262, 892–896. (10.1126/science.8235610)
  70. Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A.L. and Hartl, F.-U. (1991) Nature 352, 36–42. (10.1038/352036a0)
  71. Wu, L.C., Peng, Z.-y. and Kim, P.S. (1995) Nature Struct. Biol. 2, 281–286. (10.1038/nsb0495-281)
  72. Wu, L.C., Schulman, B.A., Peng, Z.-y. and Kim, P.S. (1996) Biochemistry 35, 859–863. (10.1021/bi951408p)
  73. Hendrix, T.M., Griko, Y. and Privalov, P. (1996) Protein Sci. 5, 923–931 (10.1002/pro.5560050514)
  74. Hornby, D.P., Whitmarsh, A., Pinabarsi, H. Kelly, S.M., Price, N.C., Shore, P.D., Baldwin, G.S. and Waltho, J. (1994) FEBS Lett. 355, 57–60. (10.1016/0014-5793(94)01171-0)
  75. Schulz, G.E. (1979) in Molecular Mechanisms of Biological Recognition (Balaban, M., ed.), pp. 79–94, Elsevier, Amsterdam.
  76. Loh, S.N., Kay, M.S. and Baldwin, R.L. (1995) Proc. Natl. Acad. Sci. USA 92, 5446–5450. (10.1073/pnas.92.12.5446)
  77. Nishii, I., Kataoka, M. and Goto, Y. (1995) J. Mol. Biol. 250, 223–238. (10.1006/jmbi.1995.0373)
  78. Missiakis, D., Betton, J.-M., Minard, P. and Yon, J.M. (1990) Biochemistry 29, 8683–8689. (10.1021/bi00489a025)
  79. Munro, A.W., Lindsay, J.G., Coggins, J.R., Kelly, S.M. and Price, N.C. (1996) Biochim. Biophys. Acta 1296, 127–137. (10.1016/0167-4838(96)00061-1)
  80. Gahn, L.G. and Roskoski, R., Jr. (1995) Biochemistry 34, 252–256. (10.1021/bi00001a030)
  81. Levinthal, C. (1968) J. Chim. Phys. 65, 44–45. (10.1051/jcp/1968650044)
  82. Dill, K.A. (1990) Biochemistry 29, 7133–7155. (10.1021/bi00483a001)
  83. Price, N.C. (1994) in Mechanisms of Protein Folding (Pain, R.H., ed.), pp. 160–193, Oxford University Press, Oxford. (10.1093/oso/9780199633968.003.0007)
  84. Kuwajima, K., Yamaya, H., Miwa, S., Sugai, S. and Nagamura, T. (1987) FEBS Lett. 221, 115–118. (10.1016/0014-5793(87)80363-0)
  85. Gilmanshin, R.I. and Ptitsyn, O.B. (1987) FEBS Lett. 223, 327–329. (10.1016/0014-5793(87)80313-7)
  86. Kalnin, N.N. and Kuwajima, K. (1995) Proteins Struct. Funct. Genet. 23, 163–176. (10.1002/prot.340230206)
  87. Jacob, M.D. and Fox, R.O. (1994) Proc. Natl. Acad. Sci. USA 91, 449–453. (10.1073/pnas.91.2.449)
  88. Goldberg, M.E., Semisotnov, G.V., Friguet, B., Kuwajima, K., Ptitsyn, O.B. and Sugai, S. (1990) FEBS Lett. 263, 51–56. (10.1016/0014-5793(90)80703-L)
  89. Mann, C.J. and Matthews, C.R. (1993) Biochemistry 32, 5282–5290. (10.1021/bi00071a002)
  90. Engelhard, M. and Evans, P.A. (1995) Protein Sci. 4, 1553–1562 (10.1002/pro.5560040813)
  91. Radford, S.E., Dobson, C.M. and Evans, P.A. (1992) Nature 358, 302–307. (10.1038/358302a0)
  92. Dobson, C.M., Evans, P.A. and Radford, S.M. (1994) Trends Biochem. Sci. 19, 31–37. (10.1016/0968-0004(94)90171-6)
  93. Neubert, L.A. and Carmack, M. (1974) J. Am. Chem. Soc. 96, 943–945. (10.1021/ja00810a065)
  94. Kishore, R., Raghothama, S. and Balaram, P. (1988) Biochemistry 27, 2462–2471. (10.1021/bi00407a032)
  95. Guijarro, J.I., Jackson, M., Chaffotte, A.F., Delepierre, M., Mantsch, H.H. and Goldberg, M.E. (1995) Biochemistry 34, 2998–3008. (10.1021/bi00009a031)
  96. Elöve, G.A., Chaffotte, A.F., Roder, H. and Goldberg, M.E. (1992) Biochemistry 31, 6876–6883. (10.1021/bi00145a003)
  97. Varley, P., Gronenborn, A.M., Christensen, H., Wingfield, P.T., Pain, R.H. and Clore, G.M. (1993) Science 260, 1110–1113. (10.1126/science.8493553)
  98. Chaffotte, A.F., Cadieux, C., Guillou, Y. and Goldberg, M.E. (1992) Biochemistry 32, 4303–4308. (10.1021/bi00132a022)
  99. Agashe, V.R., Shastry, M.C.R. and Udgaonkar, J.B. (1995) Nature 377, 754–757. (10.1038/377754a0)
  100. Dyson, H.J. and Wright, P.E. (1991) Annu. Rev. Biophys. Biophys. Chem. 20, 519–538. (10.1146/annurev.bb.20.060191.002511)
  101. Brown, J.E. and Klee, W.A. (1971) Biochemistry 10, 470–476. (10.1021/bi00779a019)
  102. Muga, A., Surewicz, W.K., Wong, P.T.T., Mantsch, H.H., Singh, V.K., Shinohara, T. (1990) Biochemistry 29, 2925–2930. (10.1021/bi00464a006)
  103. Oas, T.G. and Kim, P.S. (1988) Nature 336, 42–48. (10.1038/336042a0)
  104. Fezoui, Y., Weaver, D.L. and Osterhout, J.J. (1994) Proc. Natl. Acad. Sci. USA 91, 3675–3679. (10.1073/pnas.91.9.3675)
  105. Minor, D.L., Jr. and Kim, P.S. (1996) Nature 380, 730–734. (10.1038/380730a0)
  106. Hamada, D., Kuroda, Y., Tanaka, T. and Goto, Y. (1995) J. Mol. Biol. 254, 737–746. (10.1006/jmbi.1995.0651)
  107. Zitzewitz, J.A., Bilsel, O., Luo, J., Jones, B.E. and Matthews, C.R. (1995) Biochemistry 34, 12812–12819. (10.1021/bi00039a042)
  108. Weissman, J.S. (1995) Chem. Biol. 2, 255–260. (10.1016/1074-5521(95)90044-6)
  109. Matthews, C.R. (1993) Annu. Rev. Biochem. 62, 653–683. (10.1146/annurev.bi.62.070193.003253)
  110. Schindler, T., Herrler, H., Marahiel, M.A. and Schmid, F.X. (1995) Nature Struct. Biol. 2, 663–673. (10.1038/nsb0895-663)
  111. Kragelund, B.B., Robinson, C.V., Knudsen, J., Dobson, C.M. and Poulsen, F.M. (1995) Biochemistry 34, 7217–7224. (10.1021/bi00021a037)
  112. Sosnick, T.R., Mayne, L. and Englander, S.W. (1996) Proteins: Struct. Funct. Genet. 24, 413–426. (10.1002/(SICI)1097-0134(199604)24:4<413::AID-PROT1>3.0.CO;2-F)
  113. Fersht, A.R., Itzhaki, L.S., El Masry, N.F., Matthews, J.M. and Otzen, D.E. (1994) Proc. Natl. Acad. Sci. USA 91, 10426–10429. (10.1073/pnas.91.22.10426)
  114. Schmid, F.X., Mayr, L.M., Mucke, M. and Schonbrunner, E.R. (1993) Adv. Protein Chem. 44, 25–66. (10.1016/S0065-3233(08)60563-X)
  115. Goldenberg, D.P. (1992) Trends Biochem. Sci. 17, 257–261. (10.1016/0968-0004(92)90405-X)
  116. Freedman, R.B., Hirst, T.R. and Tuite, M.F. (1994) Trends Biochem. Sci. 19, 331–336. (10.1016/0968-0004(94)90072-8)
  117. Hayer-Hartl, M.K. and Hartl, F.-U. (1993) FEBS Lett. 320, 83–84. (10.1016/0014-5793(93)81663-K)
  118. Kraulis, J.P. (1991) J. Appl. Crystallogr. 24, 946–950. (10.1107/S0021889891004399)
Dates
Type When
Created 23 years, 1 month ago (July 26, 2002, 12:31 a.m.)
Deposited 1 year, 8 months ago (Jan. 2, 2024, 12:32 p.m.)
Indexed 2 days, 19 hours ago (Sept. 3, 2025, 6:30 a.m.)
Issued 28 years, 5 months ago (April 1, 1997)
Published 28 years, 5 months ago (April 1, 1997)
Published Print 28 years, 5 months ago (April 1, 1997)
Funders 0

None

@article{Kelly_1997, title={The application of circular dichroism to studies of protein folding and unfolding}, volume={1338}, ISSN={0167-4838}, url={http://dx.doi.org/10.1016/s0167-4838(96)00190-2}, DOI={10.1016/s0167-4838(96)00190-2}, number={2}, journal={Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology}, publisher={Elsevier BV}, author={Kelly, Sharon M and Price, Nicholas C}, year={1997}, month=apr, pages={161–185} }