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Fourier transform infrared spectroscopy for sepia melanin

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dc.contributor.author Mbonyiryivuze, A
dc.contributor.author Mwakikunga, Bonex W
dc.contributor.author Dhlamini, SM
dc.contributor.author Maaza, M
dc.date.accessioned 2016-06-27T08:41:19Z
dc.date.available 2016-06-27T08:41:19Z
dc.date.issued 2015-08
dc.identifier.citation Mbonyiryivuze, A. Mwakikunga, B. Dhlamini, S.M. and Maaza, M. 2015. Fourier transform infrared spectroscopy for sepia melanin. Physics and Materials Chemistry, 3(2), 25-29 en_US
dc.identifier.issn 2372-7098
dc.identifier.uri http://pubs.sciepub.com/pmc/3/2/2/
dc.identifier.uri http://hdl.handle.net/10204/8587
dc.description Copyright: 2015 Science and Education Publishing en_US
dc.description.abstract Melanin is of interest as a model system of understanding disorder in biological systems. The biological functionality of melanin depends on disorder which is considered as its essential part. This property distinguishes melanin from other much more intensively studied biomolecule systems such as nucleic acid, proteins and carbohydrates. Melanins have been reported to have a diverse number of functions in the biosystem, including photosensitization, metal ion chelation, photoprotection to absorb a broad range of electromagnetic radiation, antibiotic, thermoregulation. Melanins are found all over the body from the skin and blood to the nervous system but the role of melanin in all these system is unclear. FTIR spectroscopy technique is usually one of the most preferred techniques used to give a correct assignment of the observed spectral characteristic of functional groups corresponding to different absorption bands which are responsible of the absorption. FTIR is the characterization technique which is both rapid, non-destructive and requires small sized samples. In the material to be analysed, chemical bonds vibrate at a characteristic frequency representative of their structure, bond angle and length. FTIR spectrometer is important for the interpretation of the structure, binding capacity, affinity and sites of metal ions in melanin. These are important factors for better understanding the metals melanin complexity and its consequences. The analysis of sepia melanin by FTIR reveals that there is existence of functional groups that can be responsible for the binding cites of different metallic ions leading to many new applications of sepia melanin. en_US
dc.language.iso en en_US
dc.publisher Science and Education Publishing en_US
dc.relation.ispartofseries Workflow;16342
dc.subject Biological systems en_US
dc.subject Nucleic acid en_US
dc.subject Metal ion chelation en_US
dc.subject Proteins en_US
dc.subject Carbohydrates en_US
dc.subject Photoprotection en_US
dc.subject Chemical bonds en_US
dc.title Fourier transform infrared spectroscopy for sepia melanin en_US
dc.type Article en_US
dc.identifier.apacitation Mbonyiryivuze, A., Mwakikunga, B. W., Dhlamini, S., & Maaza, M. (2015). Fourier transform infrared spectroscopy for sepia melanin. http://hdl.handle.net/10204/8587 en_ZA
dc.identifier.chicagocitation Mbonyiryivuze, A, Bonex W Mwakikunga, SM Dhlamini, and M Maaza "Fourier transform infrared spectroscopy for sepia melanin." (2015) http://hdl.handle.net/10204/8587 en_ZA
dc.identifier.vancouvercitation Mbonyiryivuze A, Mwakikunga BW, Dhlamini S, Maaza M. Fourier transform infrared spectroscopy for sepia melanin. 2015; http://hdl.handle.net/10204/8587. en_ZA
dc.identifier.ris TY - Article AU - Mbonyiryivuze, A AU - Mwakikunga, Bonex W AU - Dhlamini, SM AU - Maaza, M AB - Melanin is of interest as a model system of understanding disorder in biological systems. The biological functionality of melanin depends on disorder which is considered as its essential part. This property distinguishes melanin from other much more intensively studied biomolecule systems such as nucleic acid, proteins and carbohydrates. Melanins have been reported to have a diverse number of functions in the biosystem, including photosensitization, metal ion chelation, photoprotection to absorb a broad range of electromagnetic radiation, antibiotic, thermoregulation. Melanins are found all over the body from the skin and blood to the nervous system but the role of melanin in all these system is unclear. FTIR spectroscopy technique is usually one of the most preferred techniques used to give a correct assignment of the observed spectral characteristic of functional groups corresponding to different absorption bands which are responsible of the absorption. FTIR is the characterization technique which is both rapid, non-destructive and requires small sized samples. In the material to be analysed, chemical bonds vibrate at a characteristic frequency representative of their structure, bond angle and length. FTIR spectrometer is important for the interpretation of the structure, binding capacity, affinity and sites of metal ions in melanin. These are important factors for better understanding the metals melanin complexity and its consequences. The analysis of sepia melanin by FTIR reveals that there is existence of functional groups that can be responsible for the binding cites of different metallic ions leading to many new applications of sepia melanin. DA - 2015-08 DB - ResearchSpace DP - CSIR KW - Biological systems KW - Nucleic acid KW - Metal ion chelation KW - Proteins KW - Carbohydrates KW - Photoprotection KW - Chemical bonds LK - https://researchspace.csir.co.za PY - 2015 SM - 2372-7098 T1 - Fourier transform infrared spectroscopy for sepia melanin TI - Fourier transform infrared spectroscopy for sepia melanin UR - http://hdl.handle.net/10204/8587 ER - en_ZA


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