Soluble spin labels, which "bleach" the surface proton resonances of a protein to n.m.r. measurements, can provide useful information about protein conformation and dynamics. The use of the soluble nitroxide, TEMPOL, has been explored to show the correlation of the paramagnetic perturbations of protein two-dimensional n.m.r. data with proton exposure to the free radical in hen egg-white lysozyme. The results demonstrate that the nitroxide approaches the protein randomly, and that the extent of the observed paramagnetic effects reflects the native folding pattern of the protein. A correlation of spectral simplification with the known tertiary structure establishes the feasibility of new strategies for topological mapping of surface and burie...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
Soluble spin labels, which "bleach" the surface proton resonances of a protein to n.m.r. measurement...
Soluble spin labels, which "bleach" the surface proton resonances of a protein to n.m.r. measurement...
Soluble spin labels, which "bleach" the surface proton resonances of a protein to n.m.r. measurement...
Soluble spin labels, which "bleach" the surface proton resonances of a protein to n.m.r. measurement...
We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992)....
We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992)....
We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992)....
We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992)....
We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992)....
We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992)....
In the absence oi specific interactions, the relative attenuation of protein NMR signals due to adde...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
Soluble spin labels, which "bleach" the surface proton resonances of a protein to n.m.r. measurement...
Soluble spin labels, which "bleach" the surface proton resonances of a protein to n.m.r. measurement...
Soluble spin labels, which "bleach" the surface proton resonances of a protein to n.m.r. measurement...
Soluble spin labels, which "bleach" the surface proton resonances of a protein to n.m.r. measurement...
We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992)....
We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992)....
We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992)....
We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992)....
We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992)....
We have suggested elsewhere the use of surface mapping by spin label probes (Esposito et al., 1992)....
In the absence oi specific interactions, the relative attenuation of protein NMR signals due to adde...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...
In the absence of specific interactions, the relative attenuation of protein NMR signals due to adde...