Abstract
Three final exams, two term papers, and an oral presentation—plus, you still need to clean your room and pack for a summer trip. The end of the semester is a blizzard of activity, pulling you in a hundred directions at once. It can be so overwhelming that you sometimes don’t know where to begin. One of the best strategies for coping with the chaos is to make a “to-do list,” start from the top of the list, and then attack each item one by one. Breaking down a jam-packed schedule like this creates order and organization, making the entropy more manageable and the tasks less formidable.
Sometimes ignorance is not really such a bad thing.
Attila Szabo
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Notes
- 1.
Measuring T 1 and T 2 is not too complicated. You essentially record multiple 1H-15N HSQC spectra with an increasing delay inserted in the sequence to allow either transverse or longitudinal relaxation. However, for the sake of clarity, simplicity, and length in this book, we direct the reader to pp. 315–325 in Spin Dynamics by Malcolm H. Levitt (Wiley, 2002).
References and Further Reading
Barbato G, Ikura M, Kay LE, Pastor RW, Bax A (1992) Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy. Biochemistry 31:5269–5278.
Cavanagh J, Fairbrother WJ, Palmer AGIII, Rance M, Skeleton NJ (2007) Protein NMR spectroscopy: principles and practice, 2nd edn., Chap. 8. Academic Press, Amerstdam.
Clore GM, Szabo A, Bax A, Kay LE, Driscoll PC, Gronenborn AM (1990) Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic resonance of proteins. J Am Chem Soc 112:4989–4991.
Lipari G, Szabo A (1982) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules 1. Theory and range of validity. J Am Chem Soc 104:4546–4559.
Mittermaier A, Kay LE (2006) New tools provide new insights in NMR studies of protein dynamics. Science 312:224–228.
Mittermaier A, Kay LE (2009) Observing biological dynamics at atomic resolution using NMR. Trends Biochem Sci 34:601–611.
Neudecker P, Lundström P, Kay LE (2009) Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding. Biophys J 96:2045–2054.
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© 2011 Springer-Verlag Berlin Heidelberg
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Doucleff, M., Hatcher-Skeers, M., Crane, N.J. (2011). Protein Dynamics. In: Pocket Guide to Biomolecular NMR. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-16251-0_6
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DOI: https://doi.org/10.1007/978-3-642-16251-0_6
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