Characterization of tertiary interactions in a folded protein by NMR methods: studies of pH-induced structural changes in human growth hormone

The pH-induced conformational changes in human growth hormone (hGH) have been studied, using a new quantitative NMR approach that combines 13C labeling of specific backbone carbonyl carbons with a complete spectral analysis of the corresponding 13C resonances. Thus, a complete analysis of the carbon...

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Veröffentlicht in:	Biochemistry (Easton) 1992-09, Vol.31 (36), p.8587-8596
Hauptverfasser:	Abildgaard, Frits, Joergensen, Anne Marie Munk, Led, Jens J, Christensen, Thorkild, Jensen, Ejnar B, Junker, Flemming, Dalboege, Henrik
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Biological and medical sciences Fundamental and applied biological sciences. Psychology Humans Hydrogen-Ion Concentration Leucine - chemistry Magnetic Resonance Spectroscopy - methods Models, Molecular Molecular biophysics Molecular Sequence Data Protein Conformation Somatostatin - chemistry
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