Gaggelli E, Basosi R, Pogni R, Valensin G
Department of Chemistry, University of Siena, Italy.
J Inorg Biochem. 1988 Jan;32(1):7-12. doi: 10.1016/0162-0134(88)80011-4.
The predominant species in water solution of excess carnosine and Cu2+ ions was characterized by measuring 13C and 1H spin-lattice and spin-spin relaxation rates. Four peptide molecules were calculated to be coordinated to the metal through the imidazole nitrogen. Evaluation of ion-proton distances demonstrated that metal complexation does not involve severe changes in conformation of the peptide.
通过测量¹³C和¹H的自旋晶格弛豫率以及自旋-自旋弛豫率，对过量肌肽与Cu²⁺离子水溶液中的主要物种进行了表征。经计算，四个肽分子通过咪唑氮与金属配位。离子-质子距离的评估表明，金属络合过程中肽的构象没有发生严重变化。
