To cite this paper use one of the standards below:
The biochemical function of metal ions in many processes is of fundamental importance, both in the human body and in optoelectronic devices. Most metal cations in living organisms interact with proteins, and therefore the study of metal-protein binding sites has attracted much attention in scientific research. Amino acids, which contain proton-donating groups (carboxylic acid, -COO) and proton-accepting groups (amino, -NH2), are fascinating organic materials for applications in semi-organic nonlinear optical (NLO) crystals. Single crystals of amino acids complexed with transition metals exhibit several important physical properties, such as optical (especially nonlinear optics), piezoelectric, and ferroelectric properties. These studies also contribute to the understanding of neurodegenerative diseases, such as Parkinson's, Alzheimer's and Creutzfeldt-Jakob Disease. The zwitterionic characteristic of amino acid molecules facilitates the manipulation of this substance. In this context, the present study was dedicated to the characterization, by X-ray diffraction as a function of temperature and Raman Spectroscopy, of pure and complexed crystals of Nickel L-Histidinate, Nickel L-Alaninate and Copper D-Alaninate, grown by the method of slow evaporation of an aqueous solution, with the aim of enriching studies in this field.
With nearly 200,000 papers published, Galoá empowers scholars to share and discover cutting-edge research through our streamlined and accessible academic publishing platform.
Learn more about our products:
This proceedings is identified by a DOI , for use in citations or bibliographic references. Attention: this is not a DOI for the paper and as such cannot be used in Lattes to identify a particular work.
Check the link "How to cite" in the paper's page, to see how to properly cite the paper