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Two complementary new experiments, which allow backbone assignments with good sensitivity for large deuterated proteins are presented. A 3D intra-HNCA experiment provides uniquely the intraresidue connection, while a 3D DQ-HNCA experiment, which detects a (super 13)C(super alpha)(sub i)(super 13)C(super alpha)(sub i-1) double-quantum (DQ) coherence, contains the sequential information.

The feasibility of using partial random deuteration to improve the sensitivity of a class of three- and four-dimensional nuclear magnetic resonance (NMR) experiments used in assigning the sidechain H and C resonances of proteins is studied. Results suggest that a deuteration level of 50% is enough to optimize the sensitivity of the NMR experiments by correlating the resonances of the proteins with the resonances from the backbone nuclei.

Fabrication and characterization of the crystalline self-assembled monolayers (SAMs) of organosilane compounds such as octadecyltrimethoxysilane (OTMS) and octadecyltrichlorosilane (OTCS) deposited by a simple, spin-casting technique onto Si/Si[O.sub.2] substrates is demonstrated. The characterization showed the monolayers to exhibit a well-packed crystalline phase and a remarkably high degree of smoothness.

Research is presented concerning the importance of hydrogen bonds in the retention of the three-dimensional conformations of molecules of nucleic acids and proteins. The role of hydrogen bonds in enzymatic reactions and ligand recognition are discussed.