
Peptides in BioNMR Research
Author(s) -
Oliver Zerbe,
Christian Baumann,
Matthias Schuster,
Kerstin Moehle,
Kathryn K Oi,
Erich Michel
Publication year - 2021
Publication title -
chimia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.387
H-Index - 55
eISSN - 2673-2424
pISSN - 0009-4293
DOI - 10.2533/chimia.2021.505
Subject(s) - heteronuclear molecule , allosteric regulation , chemistry , peptide , heteronuclear single quantum coherence spectroscopy , folding (dsp implementation) , biosynthesis , biochemistry , biophysics , combinatorial chemistry , nuclear magnetic resonance spectroscopy , stereochemistry , receptor , biology , enzyme , electrical engineering , engineering
Heteronuclear NMR in combination with isotope labelling is used to study folding of polypeptides induced by metals in the case of metallothioneins, binding of the peptidic allosteric modulator ?-TIA to the human G-protein coupled ?1b adrenergic receptor, the development of therapeutic drugs that interfere with the biosynthesis of the outer membrane of Gram-negative bacteria, and a system in which protein assembly is induced upon peptide addition. NMR in these cases is used to derive precise structural data and to study the dynamics.