Strategie NMR wyznaczania struktur białek w roztworze

Ejchart, A.

Artykuł - szczegóły

Tytuł artykułu

Strategie NMR wyznaczania struktur białek w roztworze

Autorzy

Ejchart A.

Wybrane pełne teksty z tego czasopisma

Identyfikatory

Warianty tytułu

NMR strategies for the protein structure determination in solution

Języki publikacji

Abstrakty

A number of reasons have hindered the use of NMR spectroscopy as a tool for the protein structure determination. Recently, the advance in the NMR equipment, spectral techniques and isotope labelling has resulted in an enormous growth of NMR-determined protein structures. After a brief presentation of protein structure and conformation several types of NMR-derived constraints and the characteristic features of chemical shifts in proteins are discussed. Short-range, distance and dihedral angle constraints are valuable, but cumulative errors can appear when succesive constraints are used to determine spatial relationship of remote parts of a protein. Therefore, long-range constraints derived from residual dipolar couplings are highly complementary to the short-range constraints. Modern strategies to the NMR-based protein structure determination depend on the size of studied biomolecules. Small proteins (M_cz< 10 kDa) can be studied with the use of two-dimensional (2D) ¹H NMR techniques. Medium size proteins (M_cz < 30 kDa) require double isotopic labeling ¹⁵N/¹³C and multidimensional (3D and 4D) heteronuclear techniques. There is no well established strategy to the structure determination of large proteins (M_cz > 30 kDa) yet. The most promising approaches take advantage of triple isotopic labeling ¹⁵N/¹³C/²H and the transverse relaxation optimized spectroscopy (TROSY), both resulting in the reduction of signal width.

Słowa kluczowe

spektroskopia NMR struktury białek w roztworach więzy strukturalne NMR

NMR spectroscopy protein structure in solution NMR structural constrains

Wydawca

Polskie Towarzystwo Chemiczne

Czasopismo

Wiadomości Chemiczne

Rocznik

2005

Tom

[Z] 59, 1-2

Strony

23--45

Opis fizyczny

Bibliogr. 46 poz., wykr.

Twórcy

autor

Ejchart A.

Instytut Biochemii i Biofizyki PAN, Pawińskiego 5A, 02-106 Warszawa

Bibliografia

[1] H. Friebolin, Basic One-and Two-Dimensional NMR Spectroscopy. 3rd revised edition, VCH Publishers Inc., Weinheim, 1999.
[2] A. Ejchart, A. Gryff-Keller, NMR w cieczach. Zarys teorii i metodologii. Oficyna Wydawnicza Politechniki Warszawskiej, Warszawa 2004.
[3] I. Zhukov, A. Ejchart, Polimery, 2003,48,28.
[4] L. Stryer, Biochemia, PWN, Warszawa 1997, rozdz. 2.
[5] K. Wuthrich, NMR of Proteins and Nucleic Acids, Wiley, New York 1986.
[6] D.A. Case, H.J. Dyson, P.E. Wright, [w:] Methods in Enzymology, red. T.L. James, N.J. Oppenheimer, tom 239, Academic Press, London 1994, s. 392.
[7] J. Rizo, L.M. Gierasch, [w:] Encyclopedia of Nuclear Magnetic Resonance, red. D.M. Grant, R.K. Harris, tom 6, John Wiley, Chichester 1996, s. 3517.
[8] A. Ejchart, Bull. Pol. Ac.: Chem., 1999, 47, 1.
[9] A.J. Dingley, E Cordier, V.A. Jaravine, S. Grzesiek, [w:] BioNMR in Drug Research, red. O. Zerbe, Wiley-VCH, Weinheim 2003, s. 207.
[10] J.H. Prestegard, J.R. Tolman, H.M. Al-Hashimi, M. Andrec, [w:] Biological Magnetic Resonance, red. N.R. Krishna, LJ. Berliner, tom 17, Kluver, New York 1999, s. 311.
[11] E. Brunner, Concepts Magn. Reson., 2001,13,238.
[12] A. Bax, G. Kontaxis, N. Tjandra, [w:] Methods in Enzymology, red. T.L. James, V. Dotsch, U. Schmitz, vol. 339, Academic Press, San Diego 2001, s. 127.
[13] E. de Alba, N. Tjandra, Prog. NMR Spectrosc., 2002,39,175.
[14] A. Bax, Protein Sei., 2003,12,1.
[15] P.J. Kraulis, J. Mol. Biol., 1994, 243,696.
[16] D.S. Wishart, B.D. Sykes, F.M. Richards, Biochemistry, 1992,31, 1647.
[17] D.S. Wishart, B.D. Sykes, J. Biomol. NMR, 1994, 4, 171.
[18] G. Comilescu, F. Delaglio, A. Bax, J. Biomol. NMR, 1999,13, 289.
[19] R. Kaptein, R. Boelens, R.M. Scheek, W.F. van Gunsteren, Biochemistry, 1988,27, 5389.
[20] G.M. Clore, A.M. Gronenbom, [w:] Biological Magnetic Resonance, red. N.R. Krishna, L.J. Berliner, tom 16, Kluver, New York 1998, s. 3.
[21] H.J. Dyson, G.P. Gippert, D.A. Case, A. Holmgren, P.E. Wright, Biochemistry, 1990,29,412.
[22] L.-Y. Lian, D.A. Middleton, Prog. NMR Spectrosc., 2001,39,171.
[23] H. Patzelt, N. Goto, H. Iwai, K. Lundstrom, E. Fernholz, [w:] BioNMR in Drug Research, red. O. Zerbe, Wiley-VCH, Weinheim 2003, s. 1.
[24] D. Cowbum, T.W. Muir, [w:] Methods in Enzymology, red. T.L. James, V. Dotsch, U. Schmitz, vol. 339, Academic Press, San Diego 2001, s. 41.
[25] A. Bax, Acc. Chem. Res., 1993, 26, 131.
[26] V. Dotsch, [w:] BioNMR in Drug Research, red. O. Zerbe, Wiley-VCH, Weinheim 2003, s. 79.
[27] L.E. Kay, [w:] Methods in Enzymology, red. T.L. James, V. Dotsch, U. Schmitz, vol. 339, Academic Press, San Diego 2001, s. 174.
[28] L. Braunschweiler, R.R. Ernst, J. Magn. Reson., 1983, 53, 521.
[29] A. Bax, D.B. Davies, J. Magn. Reson., 1985, 65,355.
[30] W.P. Aue, E. Bartholdi, R.R. Ernst, J. Chem. Phys., 1976,64,2229.
[31] J. Jeener, B.H. Meier, P. Bachmann, R.R. Ernst, J. Chem. Phys., 1979, 71, 4546.
[32] A. Ejchart, M. Siedlecka, H. Sticht, A. Bierzyński, Bull. Pol. Ac.: Chem., 1998,46,1.
[33] M. Siedlecka, G. Goch, A. Ejchart, H. Sticht, A. Bierzyński, Proc. Natl. Acad. Sei. USA, 1999,96, 903.
[34] G.W. Vuister, A. Bax, J. Am. Chem. Soc., 1993,115, 7772.
[35] S. Grzesiek, J. Anglister, A. Bax, J. Magn. Reson., 1993, B101,114.
[36] T.M. Logan, E.T. Olejniczak, R. Xu, S.W. Fesik, FEBS Lett., 1992,314, 413
[37] G.T. Montelione, BA. Lyons, S.D. Emerson, M. Tashiro, J. Am. Chem Soc., 1992, 114,10974.
[38] S. Grzesiek, A. Bax, J. Am. Chem. Soc, 1995.117,6527.
[39] T. Yamazaki, J.D. Kay, L.E. Kay, J. Am. Chem. Soc., 1993, 115,11054.
[40] T. Szyperski, G. Wider, J.H. Bushweller, K. Wuthrich, J. Am. Chem. Soc., 1993,115,9307.
[41] W. Koźmiński, I. Zhukov, J. Biomol. NMR, 2003,26,157.
[42] B. Bersch, E. Rossy, J. Covos, B. Brutscher, J. Biomol. NMR, 2003,27,57.
[43] K. Pervushin, R. Riek, G. Wider, K Wuthrich, Proc. Natl. Acad. Sei. USA, 1997,94, 12366.
[44] M. Slazmann, K. Pervushin, G. Wider, H. Senn, K. Wuthrich, Proc. Natl. Acad. Sei. USA, 1998, 95,13585.
[45] X. Shan, K.H. Gardner, D.R. Muchandaram, N.S. Rao, C.H. Arrowsmith, L.E. Kay, J. Am. Chem. Soc., 1996,118,6570.
[46] G. Wider, K. Wuthrich, Curr. Opin. Struct. Biol., 1999,9,594.

Typ dokumentu

Bibliografia

Identyfikator YADDA

bwmeta1.element.baztech-article-BUS2-0006-0053