✍ Scribed by Harald Schwalbe
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📜 SIMILAR VOLUMES
## Abstract Mastoparan‐X, a 14‐residue peptide found in wasp venom, does not adopt a well‐defined structure in water, but it folds into an α‐helix upon addition of trifluoroethanol (TFE). At low levels of TFE, the peptide is partially folded, passing through intermediate stages of folding as the am
Recently, a new procedure for the assignment of protein 'H-nmr spectra was introduced that relies on stereochemical considerations of proton-proton distances in polypeptides and on the use of two-dimensional nmr for obtaining 'H-lH through-bond and through-space connectivity maps. In the present pap
## Abstract Complementary results from ^13^C intermolecular nuclear Overhauser effects (NOE), ^1^H^13^C heteronuclear Overhauser spectroscopy (HOSEY) and ^1^H‐NMR diffusion measurements were used for probing the structure of the first solvation shell of uridine in water. It is demonstrated that a
The DNA-binding protein HU from Bacillus stearothermophilus (HUBst) is a dimer with a molecular weight of 195 kDa that is capable of bending DNA. An x-ray structure has been determined previously [Tanaka et al. 1984) Nature, vol. 310, pp. 376-381], but no structure could be established for a large p