JOURNAL BROWSE
Search
Advanced SearchSearch Tips
A simple guide to the structural study on membrane proteins in detergents using solution NMR
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
A simple guide to the structural study on membrane proteins in detergents using solution NMR
Sim, Dae-Won; Lee, Yoo-sup; Seo, Min-Duk; Won, Hyung-Sik; Kim, Ji-hun;
  PDF(new window)
 Abstract
NMR-based structural studies on membrane proteins are appreciated quite challenging due to various reasons, generally including the narrow dispersion of NMR spectra, the severe peak broadening, and the lack of long range NOEs. In spite of the poor biophysical properties, structural studies on membrane proteins have got to go on, considering their functional importance in biological systems. In this review, we provide a simple overview of the techniques generally used in structural studies of membrane proteins by solution NMR, with experimental examples of a helical membrane protein, caveolin 3. Detergent screening is usually employed as the first step and the selection of appropriate detergent is the most important for successful approach to membrane proteins. Various tools can then be applied as specialized NMR techniques in solution that include sample deteuration, amino-acid selective isotope labeling, residual dipolar coupling, and paramagnetic relaxation enhancement.
 Keywords
NMR;membrane protein;detergent screening;deuteration;amino-acid selective isotope labeling;paramagnetic relaxation enhancement;residual dipolar coupling;
 Language
English
 Cited by
 References
1.
M. J. Gorczynski, J. Grembecka, Y. Zhou, Y. Kong, L. Roudaia, M. G. Douvas, M. Newman, I. Bielnicka, G. Baber, T. Corpora, J. Shi, M. Sridharan, R. Lilien, B. R. Donald, N. A. Speck, M.L. Brown, J. H. Bushweller, Chem. Biol. 14, 1186 (2007) crossref(new window)

2.
X. Huang, J. W. Peng, N. A. Speck, J. H. Bushweller, Nat. Struct. Biol. 6, 624 (1999) crossref(new window)

3.
M. A. Yildirim, K. I. Goh, M. E. Cusick, A. L. Barabasi, M. Vidal Nat. Biotechnol. 25, 1119 (2007) crossref(new window)

4.
J. P. Overington, B. Al-Lazikani, A. L. Hopkins, Nat. Rev. Drug Discov. 5, 993 (2006) crossref(new window)

5.
J. Deisenhofer, O Epp, K Miki, R Huber, H Michel, Nature 318, 618 (1985) crossref(new window)

6.
R. S. Prosser, F. Evanics, J. L. Kitevski, M. S. Al-Abdul-Wahid, Biochemistry 45, 8453 (2006) crossref(new window)

7.
J. M. Gluck, M. Wittlich, S. Feuerstein, S. Hoffmann, D. Willbold, B. W. Koenig. J. Am. Chem. Soc. 131, 12060 (2009) crossref(new window)

8.
R. Phillips, T. Ursell, P. Wiggins, P. Sens, Nature 459, 379 (2009) crossref(new window)

9.
J. Weigelt, J. Am. Chem. Soc. 120, 12706 (1998)

10.
J. Lipfert, L. Columbus, V. B. Chu, S.A. Lesley, S. Doniach, J. Phys. Chem. B 111, 12427 (2007)

11.
A. Galoyan, R. Srapionian, R. C. Arora, J. A. Armour, Auton. Neurosci. 92, 11 (2001) crossref(new window)

12.
P. Strop, A.T. Brunger. Protein Sci. 14, 2207 (2005) crossref(new window)

13.
B. Lorber, J. B. Bishop, L. J. DeLucas, Biochim. Biophys. Acta 1023, 254 (1990) crossref(new window)

14.
A. Chattopadhyay, E. London, Anal. Biochem. 139, 408 (1984) crossref(new window)

15.
M. Kameyama, Hokkaido Igaku Zasshi 65, 1 (1990)

16.
M. T. Lin, L.J. Sperling, H. L. Frericks Schmidt, M. Tang, R.I. Samoilova, T. Kumasaka, T. Iwasaki, S.A. Dikanov, C. M. Rienstra, R. B. Gennis, Methods 55, 370 (2011) crossref(new window)

17.
A. Helenius, D. R. McCaslin, E. Fries, C. Tanford, Methods Enzymol. 56, 734 (1979) crossref(new window)

18.
F. Nilsson, O. Soderman, P. Hansson, I. Johansson, Langmuir 14, 4050. (1998) crossref(new window)

19.
R. J. Tausk, J. van Esch, J. Karmiggelt, G. Voordouw, J. T. Overbeek, Biophys. Chem. 1, 184 (1974) crossref(new window)

20.
J. J. Chou, J. L. Baber, A. Bax, J. Biomol. NMR 29, 299 (2004) crossref(new window)

21.
R. E. Stafford, T. Fanni, E. A. Dennis, Biochemistry 28, 5113 (1989) crossref(new window)

22.
L. M. Hjelmeland, D. W. Nebert, J. C. Osborne, Jr. Anal. Biochem. 130, 72 (1983) crossref(new window)

23.
S. Park, J. Kor. Magn. Reson. Soc. 18, 47 (2014) crossref(new window)

24.
T. Torizawa, M. Shimizu, M. Taoka, H. Miyano, M. Kainosho, J. Biomol. NMR 30, 311 (2004) crossref(new window)

25.
H. W. Kim, J.A. Perez, S. J. Ferguson, I. D. Campbell, FEBS Lett. 272, 34 (1990) crossref(new window)

26.
C. O'Grady, B. L. Rempel, A. Sokaribo, S. Nokhrin, O. Y. Dmitriev, Anal. Biochem. 426, 126 (2012) crossref(new window)

27.
K. I. Tong, M. Yamamoto, T. Tanaka, J. Biomol. NMR 42, 59 (2008) crossref(new window)

28.
S. M. Douglas, J. J. Chou, W. M. Shih, Proc. Natl. Acad. Sci. U S A 104, 6644 (2007) crossref(new window)

29.
D. E. Kamen, S. M. Cahill, M. E. Girvin, J. Am. Chem. Soc. 129, 1846 (2007) crossref(new window)

30.
M. Han, J. Suh, J. Kor. Magn. Reson. Soc. 19, 61 (2015) crossref(new window)

31.
J. L. Battiste, G. Wagner, Biochemistry 39, 5355 (2000) crossref(new window)

32.
W. D. Van Horn, H. Kim, C. D. Ellis, A. Hadziselimovic, E.S. Sulistijo, M. D. Karra, C. Tian, F. D. Sonnichsen, C. R. Sanders, Science 324, 1726 (2009) crossref(new window)