Abstract: Protein structural determination using NMR techniques is improved through use of proteins in which one or more amino acids in the peptidic sequence are isotopically enriched in the sidechain with 2H and are isotopically enriched on the backbone with 13C, 15N, 2H or any combination thereof. This invention provides amino acids isotopically enriched as above, which can be used to synthesize isotopically labeled proteins and peptides for protein structural determinations by NMR, and methods for their synthesis. Other embodiments of the invention include peptidic molecules, media for peptidic molecule expression, methods of making isotopically labeled peptidic molecules and methods of determining structural information of a peptidic molecule.

Abstract: This invention provides a method for rapidly obtaining accurate three-dimensional structure of proteins including large or multi-sub unit proteins, using a combination of NMR analysis of backbone only 13C, 15N or 13C and 15N isotopically labeled proteins which are optionally also 2H isotopically labeled in the C? position protons and residual dipolar coupling measurements in more than one partially aligned state and/or orientation data pertaining to overlapping successive peptide pairs.

Abstract: This invention provides a method for rapidly obtaining accurate three-dimensional structure of proteins including large or multi-sub unit proteins, using a combination of NMR analysis of backbone only 13C, 15N or 13C and 15N isotopically labeled proteins which are optionally also 2H isotopically labeled in the C&agr; position protons and residual dipolar coupling measurements in more than one partially aligned state and/or orientation data pertaining to overlapping successive peptide pairs.

Abstract: This invention provides a method for rapidly obtaining accurate three-dimensional structure of proteins including large or multi-sub unit proteins, using a combination of NMR analysis of backbone only 13C, 15N or 13C and 15N isotopically labeled proteins which are optionally also 2H isotopically labeled in the C&agr; position protons and residual dipolar coupling measurements in more than one partially aligned state.