caa a22 4500 397557094 CHVBK 20180308164805.0 cr unu---uuuuu 161202e199607 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021373 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021373 Yamamoto Yasuhiko Department of Chemistry, University of Tsukuba, Tsukuba, Ibaraki 305 1H NMR Probes for Inter-Segmental Hydrogen Bonds in Myoglobins [Elektronische Daten] [Yasuhiko Yamamoto] NMR signals arising from the HisB5 NδH and HisEF5 NcH protons in sperm whale skeletal and horse heart myoglobins have been located for the first time in the downfield shifted portion of the spectra. The shifts and hydrogen exchange rates indicate that these His imidazole ring NH protons are involved in the inter-segmental hydrogen bonds of the protein in solution, as demonstrated by a crystallographic study [Takano, T. (1977) J. Mol. Biol. 220, 381-399]. The assigned His imidazole ring NH proton resonances can serve as new sensitive structural probes in the study of the local conformation of myoglobin. The applicability of the NMR spectral parameters in the study of the tertiary structure of apomyoglobin, the denaturation of the protein, and the protein stability of sperm whale and horse myoglobins is presented in some detail. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence apomyoglobin nationallicence hydrogen bond nationallicence myoglobin nationallicence NMR nationallicence protein folding nationallicence The Journal of Biochemistry Oxford University Press 120/1(1996-07), 126-132 0021-924X 120:1<126 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021373 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021373 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Yamamoto Yasuhiko Department of Chemistry, University of Tsukuba, Tsukuba, Ibaraki 305 NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/1(1996-07), 126-132 0021-924X 120:1<126 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford