Nuclear magnetic resonance binding interactions studied

Other supportive evidence for a specific water-solid interaction is available from thermal studies showing the amount of non-freezeable water,nuclear magnetic resonance,and diffusion studies. The evidence is less clear, however, concerning whether there is distinct binding of water to sorption sites with discrete energy levels or whether there is a continuum of states where water interacts to a lesser extent with increasing amount sorbed. In any event, it is clear that sorbed water behaves with a considerable degree of mobility, and hence, questions the use of the term bound water. ... 

Kelusky, E. C. Smith, I. C. R, Anethetic-membrane interaction A 2H nuclear magnetic resonance study of the binding of specifically deuterated tetracaine and procaine to phosphatidylcholine, Can. J. Biochem. Cell Biol. 62, 178-184 (1984). 

Nuclear magnetic resonance (NMR) spectroscopy has been applied to elucidate metal-binding mechanisms to organic ligands mainly by two approaches by measuring the effects of metal complexation on either the relaxation times of H of water molecules solvating the metal cation or on the chemical shifts of NMR-active metal ions (e.g.. Cd, Al, and Pb) (e.g., Connors, 1987 Wilson, 1989 Macomber, 1998). Relatively few and sparse studies have been performed by NMR on metal-HS complexes. A comprehensive and updated review has been provided by Kmgery et al. (2001) on the various applications of NMR spectroscopy to the study of metal-HS interactions. 

Ibere are relatively few physical techniques available for the characterization of the interaction of monovalent cations with biological molecules responsible for cation transport. However, nuclear magnetic resonance (NMR) spectroscopy has proven to be a very powerful technique for the study of the transport process and the molecular systems responsible for the transport. NMR techniques can be used to determine the three-dimensional structure of the channel, to determine the thermodynamic parameters for the incorporation of the transport system into the membrane environment, to obtain the thermodynamic parameters for the binding of the cations to the channel, to determine the kinetic activation enthalpy for the transport process, and to study the internal motion of the peptide or protein that forms the channel. 

No detailed structure information on the recognition of the third form of doublehelical DNA, the left-handed Z-DNA, by proteins is available so far. Although several Z-DNA binding proteins and antibodies have been isolated [119, 120], no protein has yet been expressed and purified to the point where X-ray crystallographic or nuclear magnetic resonance methods would allow detailed studies of proteln-DNA interactions. 

Nuclear magnetic resonance studies show structural detail of this interaction (Mornet et al., 1995 Levine etal., 1990). Amino acids 1-7 of actin interact with domain 4 but not with the C-terminal fragment 658C, thus actin 1-7 probably binds to the N terminus of domain 4, whereas the C-terminal half binds elsewhere on actin, currently not identified. A paramagnetic label attached to cysteine 636 (580) perturbs the nmr signals of histidine 667 (610), tyrosine 682 (625), and at least one of the tryptophans 716,749, or 779 (659,692, or 722), indicating that all of these residues are within 1.5 nm of the cysteine 636 (580). This means... 

C. Mihai, Study of the protein-sugar interaction in chitin binding elderberry lectin by nuclear magnetic resonance spectroscopy, PhD Thesis, Vrije Universiteit Brussel (2004). 

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