Nuclear magnetic resonance spectroscopy dynamics

Freeman R and Hiii H D W 1975 Determination of spin-spin reiaxation time in high-resoiution NMR Dynamic Nuclear Magnetic Resonance Spectroscopy e6 L M Jaokman and F A Cotton (New York Aoademio) p 131-62... 

Jaokman L M and Cotton F A 1975 Dynamic Nuclear Magnetic Resonance Spectroscopy (New York Aoademio)... 

Gutowsky H S and Holm C H 1975 Time-dependent magnetic perturbations Dynamic Nuclear Magnetic Resonance Spectroscopy ed L M Jackman and F A Cotton (New York Academic) pp 1-21... 

BalK82 Balasubramanian, K. Topological and group theoretical analysis of dynamics nuclear magnetic resonance spectroscopy. J. Phys. Chem. 86 (1982) 4668-4674. 

Finally, Burkhard Luy, Andreas Frank and Horst Kessler discuss Conformational Analysis of Drugs by Nuclear Magnetic Resonance Spectroscopy . The determination and refinement of molecular conformations comprehends three main methods distance geometry (DG), molecular dynamics (MD) and simulated anneahng (SA). In principle, it is possible to exclusively make use of DG, MD or... 

Nuclear magnetic resonance spectroscopy for /V-acyloxy-/V-alkoxyamides 13C NMR spectroscopy, 56-58 15N NMR spectroscopy, 58-59 dynamic 1H NMR spectroscopy, 59 Nucleophilic substitution (SN2) reactions, /V-acyloxy-/V-alkoxyamidcs, 70-90 alcoholysis reactions, 89-90 with aromatic amines, HERON reactions, 70-74... 

Binsch, G. Band-Shape Analysis." In Dynamic Nuclear Magnetic Resonance Spectroscopy Jackman, L. M. Cotton, F. A., Eds. Academic Press New York, 1975 pp. 45-81. See also Binsch, G. Top Stereochem., 1968, 3, 97-192. 

G. Binsch in Dynamic Nuclear Magnetic Resonance Spectroscopy, L. M. Jackman and F. A. Cotton, eds. Academic Press, NY, 1975, Chap. 3. 

To detect dynamic featnres of colloidal preparations, additional methods are required. Nuclear magnetic resonance spectroscopy allows a rapid, repeatable, and noninvasive measurement of the physical parameters of lipid matrices withont sample preparation (e.g., dilution of the probe) [26,27]. Decreased lipid mobility resnlts in a remarkable broadening of the signals of lipid protons, which allows the differentiation of SLN and supercooled melts. Because of the different chemical shifts, it is possible to attribute the nuclear magnetic resonance signal to particnlar molecnles or their segments. 

A reevaluation of molecular structure of humic substances based on data obtained primarily from nuclear magnetic resonance spectroscopy, X-ray absorption near-edge structure spectroscopy, electrospray ionization-mass spectrometry, and pyrolysis studies was presented by Sutton and Sposito (2005). The authors consider that humic substances are collections of diverse, relatively low molecular mass components forming dynamic associations stabilized by hydrophobic interactions and hydrogen bonds. These associations are capable of organizing into micellar structures in suitable aqueous environments. Humic components display contrasting molecular motional behavior and may be spatially segregated on a scale of nanometers. Within this new structural context, these components comprise any molecules... 

Nuclear magnetic resonance spectroscopy of dilute polymer solutions is utilized routinely for analysis of tacticlty, of copolymer sequence distribution, and of polymerization mechanisms. The dynamics of polymer motion in dilute solution has been investigated also by protoni - and by carbon-13 NMR spectroscopy. To a lesser extent the solvent dynamics in the presence of polymer has been studied.Little systematic work has been carried out on the dynamics of both solvent and polymer in the same systan. 

C. Thomas, C. Counsell, P. Wood, G.E. Adams, Use of F-19 nuclear-magnetic-resonance spectroscopy and hydralazine for measuring dynamic changes in blood perfusion volume in tumors in mice, J. Natl. Cancer Inst. 84 (1992) 174-180. 

The newly evolving ideas of a protein differ from those that can be generated from the X-ray structure mainly because they are dynamic and not static in nature. Nuclear magnetic resonance spectroscopy (nmr) is the technique that is revealing the most detail about the dynamic aspects of protein structure, and much of this article is concerned with the results of nmr studies. It is unfortunately the case that dynamic models are much the more difficult to describe and to use in a precise way, but it is very important to realize that quite a new outlook on a protein has to be developed. The dynamics of a protein structure are now known to be specific to a given protein, and the response of the protein to external changes, either physical or chemical, is therefore specific also. 

McEvoy, M.M. Muhandiram, D.R. Kay, L.E. Dahlquist, F.W. Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. Biochemistry, 35, 5633-5640 (1996)... 

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