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A solution NMR-based studies which provide insight into the structure, function, and dynamics of 15.5K in the Kink-turn protein-RNA interaction is described.

The effects of low temperature and ionic strength on water encapsulated within reverse micelles are investigated by solution NMR. The results obtained demonstrate that reverse micelle is an excellent vehicle for studies of confined water across a broad range of conditions, including the temperature range that provides access to the supercooled state.

Research has been conducted on the small acidic protein, calmodulin which acts as an intracellular calcium sensor protein. The structural dynamics and energetics of interactions of a peptide and calcium-saturated calmodulin have been investigated via the amide hydrogen exchange and the results are reported.

Research has been conducted on the Cyanobacterium anabaena oxidized flavodoxin. The use of this flavodoxin in investigating the internal dynamics of the flavin-bearing protein is described.

Research has been conducted on the main chain and side chain dynamics in Rhodobacter capsulatus ferrocytochrome c (sub)2. The use of deuterium relaxation in side chain methyl groups which provide detailed measure of internal dynamics has been examined.

2H and 13C NMR relaxation techniques used in studying the dynamics of methyl groups in proteins have been compared against each other. These methods were used in measuring the field dependence of carbon and deuterium relaxation parameters. Results indicate that both spectroscopic types obtained similar principal features of ps-ns side chain dynamics. It was observed that the 2H approach is more efficient in determining the degree of spatial restriction of the methyl symmetry axis. However, the broad frequency distribution of 13C relaxation was able to distinguish fast methyl rotation from symmetry axis reorientation.

The chemical shift perturbation analysis of the amide [super 1]H and [super 15]N resonances were used to monitor the effects of encapsulation on ubiquitin encapsulated within bis(2-ethylhexyl) sodium sulfosuccinate AOT reverse micelles under various degrees of confinement. The study data provide an important bridge between commonly employed dilute in vitro studies and studies of the effects of a crowded environment as well as reconcile alternative interpretations of protein cold denaturation within reverse micelles.

Encapsulation with surfactant-based reverse micelles is an effective biophysical tool that can be used for studying the effect of ionic strength, pH, hydration and crowding on biologically active macromolecules over a wide range of conditions. The results have shown that RNA oligonucleotides have acquired significant stability in the presence of cellular levels of crowding.

The influence of encapsulation on the backbone dynamics in the well-studied and representative protein ubiquitin is investigated. The results have shown that the dynamics of ubiquitin in a reverse micelle are similar to results obtained in solution state, with slight decreases in the amplitude of fast local motion in regions of the molecule that are associated with increased structural flexibility.

Ubiquitin encapsulated within Aerosol-OT (AOT) reverse micelles is studied using multidimensional multinuclear solution NMR to determine the relationship between protein structure, temperature, and ionic strength. The results indicate that the structure of the encapsulated protein at low temperature experiences perturbation arising from two major influences, which are reverse micelle-protein interactions and low-temperature effects.

Protein structure in encapsulated proteins dissolved in low viscosity fluids was studied.

Research is presented describing the nuclear magnetic resonance study of proteins using cryogenic probe technology.

High-pressure triple-resonance NMR spectroscopy was employed to monitor the contributions of hydrophobic and ionic interactions on the affinity and specificity of an apocalmodulin.neuro-p complex. The results, which showed strong crosspeaks in the N-HSQC spectra of the peptide due to hydrogen bonding with apocalmodulin, support the theory that hydrophobic interactions play a controlling role in the affinity of such complexes.