EurekaMag
+ Translate
+ Most Popular
Cunninghamia lanceolata plantations in China
Mammalian lairs in paleo ecological studies and palynology
Studies on technological possibilities in utilization of anhydrous milk fat for production of recombined butter-like products
Should right-sided fibroelastomas be operated upon?
Large esophageal lipoma
Apoptosis in the mammalian thymus during normal histogenesis and under various in vitro and in vivo experimental conditions
Poissons characoides nouveaux ou non signales de l'Ilha do Bananal, Bresil
Desensitizing efficacy of Colgate Sensitive Maximum Strength and Fresh Mint Sensodyne dentifrices
Administration of fluid by subcutaneous infusion: revival of a forgotten method
Tundra mosquito control - an impossible dream?
Schizophrenia for primary care providers: how to contribute to the care of a vulnerable patient population
Geochemical pattern analysis; method of describing the Southeastern limestone regional aquifer system
Incidence of low birth weights in a hospital of Mexico City
Tabanidae
Graded management intensity of grassland systems for enhancing floristic diversity
Microbiology and biochemistry of cheese and fermented milk
The ember tetra: a new pygmy characid tetra from the Rio das Mortes, Brazil, Hyphessobrycon amandae sp. n. (Pisces, Characoidei)
Risk factors of contrast-induced nephropathy in patients after coronary artery intervention
Renovation of onsite domestic wastewater in a poorly drained soil
Observations of the propagation velocity and formation mechanism of burst fractures caused by gunshot
Systolic blood pressure in a population of infants in the first year of life: the Brompton study
Haematological studies in rats fed with metanil yellow
Studies on pasteurellosis. I. A new species of Pasteurella encountered in chronic fowl cholera
Dormancy breaking and germination of Acacia salicina Lindl. seeds
therapy of lupus nephritis. a two-year prospective study

Nuclear magnetic resonance studies of amino acids and proteins. Rotational correlation times of proteins by deuterium nuclear magnetic resonance spectroscopy


Nuclear magnetic resonance studies of amino acids and proteins. Rotational correlation times of proteins by deuterium nuclear magnetic resonance spectroscopy



Biochemistry 22(12): 2908-2913



ISSN/ISBN: 0006-2960

PMID: 6871171

DOI: 10.1021/bi00281a020

We show that measurement of the spin-lattice (T1) and spin-spin (T2) relaxation times (or line widths) of irrotationally bound 2H nuclei in macromolecules undergoing isotropic rotational motion outside of the extreme narrowing limit (i.e., for the case omega 02 tau R2 much greater than 1) permits determination of both the rotational correlation time (tau R) of the macromolecule and the electric quadrupole coupling constant (e2qQ/h) of the 2H label. The technique has the advantage over 13C nuclear magnetic resonance (NMR) that no assumptions about bond lengths (which appear to the sixth power in 13C relaxation studies) or relaxation mechanisms need to be made, since relaxation will always be quadrupolar, even for aromatic residues at high field. Asymmetry parameter (eta) uncertainties are shown to cause negligible effects on tau R determinations, and in any case it is shown that both e2qQ/h and eta may readily be determined in separate solid-state experiments. By way of example, we report 2H NMR results on aqueous lysozyme (EC 3.2.1.17) at 5.2 and 8.5 T (corresponding to 2H-resonance frequencies of 34 and 55 MHz). Interpretation of the results in terms of the isotropic rigid-rotor model yields e2qQ/h values of approximately equal to 170 or approximately equal to 190 kHz, respectively, for the imidazolium and free-base forms of [epsilon 1-2H] His-15 lysozyme in solution, in excellent agreement with e2qQ/h values of approximately 167 and approximately 190 kHz obtained for the free amino acids in the solid state. In principle, the method may in suitable cases permit comparison between the dynamic structures of proteins in solution and in the crystalline solid state.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 018032479

Download citation: RISBibTeXText

Related references

Nuclear magnetic resonance studies of amino acids and proteins. Deuterium nuclear magnetic resonance relaxation of deuteriomethyl-labeled amino acids in crystals and in Halobacterium halobium and Escherichia coli cell membranes. Biochemistry 23(2): 288-298, 1984

Nuclear magnetic resonance spectroscopy of amino acids, peptides, and proteins. Advances in Protein Chemistry 24: 447-545, 1970

First observation of amino acid side chain dynamics in membrane proteins using high field deuterium nuclear magnetic resonance spectroscopy. Journal of Biological Chemistry 256(9): 4146-4149, 1981

Solid-state deuterium nuclear magnetic resonance spectroscopy of proteins. Methods in Enzymology 176: 376-386, 1989

Carbon-13 nuclear-magnetic-resonance studies on selected amino acids, peptides, and proteins. European Journal of Biochemistry 32(2): 215-226, 1973

Dynamics of amino acid side chains in membrane proteins by high field solid state deuterium nuclear magnetic resonance spectroscopy. Phenylalanine, tyrosine, and tryptophan. Journal of Biological Chemistry 256(17): 9028-9036, 1981

Efficient incorporation of deuterated amino acids into quail egg white proteins for nuclear magnetic resonance studies. Journal of Biological Chemistry 256(4): 1506-1509, 1981

Natural-abundance, 13C-nuclear magnetic resonance-spectral studies of carbohydrates linked to amino acids and proteins. Advances in Carbohydrate Chemistry and Biochemistry 43: 1-49, 1985

Two-dimensional nuclear magnetic resonance of natural products. IV: Investigation of the solution conformation of luliberin by 1H, 13C, and 2D 1H-13C shift correlation nuclear magnetic resonance spectroscopy. Journal of the Chemical Society. Perkin Transactions. i (1): 145-148, 1984

Preliminary in vitro studies of nuclear magnetic resonance spin-lattice relaxation times and three-dimensional nuclear magnetic resonance imaging in gynecologic oncology. American Journal of Obstetrics and Gynecology 148(1): 91-95, 1984

Magnetic resonance spectroscopy of wheat proteins: a magic-angle-spinning 13C nuclear magnetic resonance and an electron spin resonance spin label study. Journal of cereal science 3(4): 319-327, 1985

Probing protein structure by solvent perturbation of nuclear magnetic resonance spectra. Nuclear magnetic resonance spectral editing and topological mapping in proteins by paramagnetic relaxation filtering. Journal of Molecular Biology 224(3): 659-670, 1992

Use of 13C and 15N isotope labels for proton nuclear magnetic resonance and nuclear Overhauser effect. Structural and dynamic studies of larger proteins and nucleic acids. Archivos de Biologia y Medicina Experimentales 22(2): 129-137, 1989

Nuclear magnetic resonance spectroscopy studies on copper proteins. Advances in Protein Chemistry 60: 397-449, 2002

The biosynthesis of isotope hybrid proteins for high resolution nuclear magnetic resonance studies by incorporation of [1H]amino acids into fully deuterated algae. Biochimica et Biophysica Acta 200(1): 26-33, 1970