This paper demonstrates that two-dimensional (2D) NMR experiments are particularly suitable for studies of biopolymers in H2O solution. Compared to conventional one-dimensional NMR experiments the 2D studies are much more efficient and yield with a single instrument setting a nearly complete network of J-connectivities or cross relaxation pathways involving labile protons. The use of these techniques in H2O solutions presents a new approach for detailed studies of the backbone spatial structure in proteins and should further be of particular interest for conformational studies of nucleic acids. Here, homonuclear J-connectivities and Overhauser effects (NOE) involving labile protons were studied in the basic pancreatic trypsin inhibitor
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
The study of the structure and behavior of biomolecules is a key step to understanding their biologi...
In the absence oi specific interactions, the relative attenuation of protein NMR signals due to adde...
It is demonstrated, by means of experiments with the basic pancreatic trypsin inhibitor, that the bu...
It is demonstrated, by means of experiments with the basic pancreatic trypsin inhibitor, that the bu...
This paper describes a new nuclear magnetic resonance approach for the determination of secondary st...
Experimental techniques used for homonuclear 2D 1H NMR studies of proteins are described. A brief su...
Experimental techniques used for homonuclear 2D 1H NMR studies of proteins are described. A brief su...
During the last 5 years, since its first application to biomolecules, twodimensional nuclear Overhau...
During the last 5 years, since its first application to biomolecules, twodimensional nuclear Overhau...
During the last 5 years, since its first application to biomolecules, twodimensional nuclear Overhau...
The conformation of the hexanucieoside pentaphosphate r(CGCGCG) in aqueous solution was studied by c...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
The development of two-dimensional proton-proton nuclear Overhauser effect spectroscopy was a semina...
The development of two-dimensional proton-proton nuclear Overhauser effect spectroscopy was a semina...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
The study of the structure and behavior of biomolecules is a key step to understanding their biologi...
In the absence oi specific interactions, the relative attenuation of protein NMR signals due to adde...
It is demonstrated, by means of experiments with the basic pancreatic trypsin inhibitor, that the bu...
It is demonstrated, by means of experiments with the basic pancreatic trypsin inhibitor, that the bu...
This paper describes a new nuclear magnetic resonance approach for the determination of secondary st...
Experimental techniques used for homonuclear 2D 1H NMR studies of proteins are described. A brief su...
Experimental techniques used for homonuclear 2D 1H NMR studies of proteins are described. A brief su...
During the last 5 years, since its first application to biomolecules, twodimensional nuclear Overhau...
During the last 5 years, since its first application to biomolecules, twodimensional nuclear Overhau...
During the last 5 years, since its first application to biomolecules, twodimensional nuclear Overhau...
The conformation of the hexanucieoside pentaphosphate r(CGCGCG) in aqueous solution was studied by c...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
The development of two-dimensional proton-proton nuclear Overhauser effect spectroscopy was a semina...
The development of two-dimensional proton-proton nuclear Overhauser effect spectroscopy was a semina...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
The study of the structure and behavior of biomolecules is a key step to understanding their biologi...
In the absence oi specific interactions, the relative attenuation of protein NMR signals due to adde...