The α-helix dipole and the properties of proteins

W. G. J. Hol; P. T. van Duijnen; H. J. C. Berendsen

doi:10.1038/273443a0

journal article Jun 01, 1978

The α-helix dipole and the properties of proteins

W. G. J. Hol P. T. van Duijnen H. J. C. Berendsen

Nature Vol. 273 No. 5662 pp. 443-446 · Springer Science and Business Media LLC

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References

41

[1]

Wada, A. Adv. Biophys. 9, 1–63 (1976).

[2]

Poland, D. & Scheraga, H. A. Biochemistry 6, 3791–3800 (1967). 10.1021/bi00864a024

[3]

Berendsen, H. J. C. Report on CECAM Workshop Models in Protein Dynamics 299–304 (CECAM, Orsay, France, 1976).

[4]

Mayhew, S. G. & Ludwig, M. L. Enzymes 12, 57–118 (1975). 10.1016/s1874-6047(08)60225-5

[5]

Moras, D. et al. J. biol. Chem. 250, 9137–9162 (1975). 10.1016/s0021-9258(19)40703-5

[6]

Biesecker, G., Ieuan Harris, J., Thierry, J. C., Walker, J. E. & Wonacott, A. J. Nature 266, 328–333 (1977). 10.1038/266328a0

[7]

Brändén, C. I., Jörnvall, H., Eklund, H. & Furugren, B. Enzymes 11, 103–190 (1975). 10.1016/s1874-6047(08)60211-5

[8]

Rossmann, M. G., Liljas, A., Brändén, C. I. & Banaszak, L. J. Enzymes 11, 61–102 (1975). 10.1016/s1874-6047(08)60210-3

[9]

Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data

D. W. Banner, A. C. Bloomer, G. A. Petsko et al.

Nature 1975 10.1038/255609a0

[10]

Hammes, G. G. & Schimmel, P. R. Enzymes 2, 67–114 (1970). 10.1016/s1874-6047(08)60181-x

[11]

Kraut, J. A. Rev. Biochem. 46, 331–358 (1977). 10.1146/annurev.bi.46.070177.001555

[12]

Robertus, J. D., Kraut, J., Alden, R. A. & Birktoft, J. J. Biochmistry 11, 4293–4303 (1972). 10.1021/bi00773a016

[13]

Glazer, A. N. & Smith, E. L. Enzymes 3, 501–546 (1971). 10.1016/s1874-6047(08)60405-9

[14]

Drenth, J., Kalk, K. H. & Swen, H. M. Biochemistry 15, 3731–3738 (1976). 10.1021/bi00662a014

[15]

Drenth, J., Swen, H. M., Hoogenstraaten, W. & Sluyterman, L. A. AE. Kon. Nederl. Akad. Wetensch. 78, 104–110 (1974).

[16]

Garavito, R. M., Rossmann, M. G., Argos, P. & Eventoff, L. W. Biochemistry 16, 5065–5071 (1977). 10.1021/bi00642a019

[17]

Ieuan Harris, J. & Waters, M. Enzymes 13, 1–49 (1976). 10.1016/s1874-6047(08)60239-5

[18]

Westley, J. Adv. Enzym. 39, 327–368 (1973).

[19]

Ploegman, J. H. et al. Nature 273, 124–129 (1978). 10.1038/273124a0

[20]

Ploegman, J. H. et al. Nature 273, 124–129 (1978). 10.1038/273124a0

[21]

Schlesinger, P. & Westley, J. J. biol. Chem. 249, 780–788 (1974). 10.1016/s0021-9258(19)42997-9

[22]

Birktoft, J. J. & Blow, D. M. J. molec. Biol. 68, 187–240 (1972). 10.1016/0022-2836(72)90210-0

[23]

Shotton, D. M. & Watson, H. C. Nature 225, 811–816 (1970). 10.1038/225811a0

[24]

Stroud, R. M., Kay, L. M. & Dickerson, R. E. J. molec. Biol. 83, 185–208 (1974). 10.1016/0022-2836(74)90387-8

[25]

Bode, W. & Schwager, P. J. molec. Biol. 98, 693–717 (1975). 10.1016/s0022-2836(75)80005-2

[26]

Delbaere, L. F. J., Hutcheon, W. L. B., James, M. N. G. & Thiessen, W. E. Nature 257, 758–763 (1975). 10.1038/257758a0

[27]

Chemical and biological evolution of a nucleotide-binding protein

Michael G. Rossmann, Dino Moras, Kenneth W. Olsen

Nature 1974 10.1038/250194a0

[28]

Eventoff, W. & Rossman, M. G. CRC Critical Reviews in Biochemistry 111–140 (1974). 10.3109/10409237509102554

[29]

Schultz, G. E. & Schirmer, R. H. Nature 250, 142–144 (1974). 10.1038/250142a0

[30]

Structural and functional similarities within the coenzyme binding domains of dehydrogenases

Ingrid Ohlsson, Bo Nordström, Carl-Ivar Brändén

Journal of Molecular Biology 1974 10.1016/0022-2836(74)90523-3

[31]

Holbrook, J. J., Liljas, A., Steindel, S. J. & Rossmann, M. G. Enzymes 11, 191–292 (1975). 10.1016/s1874-6047(08)60212-7

[32]

Watenpaugh, K. D., Sieker, L. C., Jensen, L. H., Le Gall, T. & Dubourdieu, M. Proc. natn. Acad. Sci. U.S.A. 69, 3185–3188 (1972). 10.1073/pnas.69.11.3185

[33]

Burnett, R. M. et al. J. biol. Chem. 249, 4383–4392 (1974). 10.1016/s0021-9258(19)42429-0

[34]

Olsen, K. W., Garavito, R. M., Saseban, M. N. & Rossmann, M. G. J. molec. Biol. 107, 571–576 (1976). 10.1016/s0022-2836(76)80083-6

[35]

Phillips, D. C., Rivers, P. S., Sternberg, M. J. E., Thornton, J. M. & Wilson, I. A. Biochem. Soc. Trans. 5, 642–647 (1977). 10.1042/bst0050642

[36]

Blow, D. M., Owen, M. G. & Nyburg, J. Biochem. biophys. Res. Commun. 67, 728–734 (1977). 10.1016/0006-291x(77)91560-1

[37]

Drenth, J., Jansonius, J. N., Koekoek, R. & Wolthers, B. G. Enzymes 3, 485–494 (1971). 10.1016/s1874-6047(08)60404-7

[38]

Structure of Subtilisin BPN′ at 2.5 Å Resolution

CHRISTINE SCHUBERT WRIGHT, RICHARD A. ALDEN, JOSEPH KRAUT

Nature 1969 10.1038/221235a0

[39]

Subtilisin Novo. The Three-Dimensional Structure and Its Comparison with Subtilisin BPN'

Jan Drenth, Wilhelmus G. J. Hol, J.N. Jansonius et al.

European Journal of Biochemistry 1972 10.1111/j.1432-1033.1972.tb01754.x

[40]

Matthews, D. A., Alden, R. A., Birktoft, J. J., Freer, S. T. & Kraut, J. J. biol. Chem. 250, 7120–7126 (1975). 10.1016/s0021-9258(19)40917-4

[41]

Fersht, A. Enzyme Structure and Mechanism Ch. 10 (W. H. Freeman, San Francisco and Reading, 1978).

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Published: Jun 01, 1978
Vol/Issue: 273(5662)
Pages: 443-446
License: View

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Cite This Article

W. G. J. Hol, P. T. van Duijnen, H. J. C. Berendsen (1978). The α-helix dipole and the properties of proteins. Nature, 273(5662), 443-446. https://doi.org/10.1038/273443a0

The α-helix dipole and the properties of proteins

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