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Main Authors: Bemquerer, Marcelo P., Macedo, Jessica K. A., Ribeiro, Ana Carolina J., Carvalho, Andrea C., Silva, Debora O. C., Braz, Juliana M., Medeiros, Kelliane A., Sallet, Lunalva A. P., Campos, Pollyanna F., Prates, Maura V., Silva, Luciano P.
Format: Recurso educativo Open Access
Language:en
Published: 2012
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Online Access:https://eric.ed.gov/?id=EJ990932
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author Bemquerer, Marcelo P.
Macedo, Jessica K. A.
Ribeiro, Ana Carolina J.
Carvalho, Andrea C.
Silva, Debora O. C.
Braz, Juliana M.
Medeiros, Kelliane A.
Sallet, Lunalva A. P.
Campos, Pollyanna F.
Prates, Maura V.
Silva, Luciano P.
author_facet Bemquerer, Marcelo P.
Macedo, Jessica K. A.
Ribeiro, Ana Carolina J.
Carvalho, Andrea C.
Silva, Debora O. C.
Braz, Juliana M.
Medeiros, Kelliane A.
Sallet, Lunalva A. P.
Campos, Pollyanna F.
Prates, Maura V.
Silva, Luciano P.
Bemquerer, Marcelo P.
Macedo, Jessica K. A.
Ribeiro, Ana Carolina J.
Carvalho, Andrea C.
Silva, Debora O. C.
Braz, Juliana M.
Medeiros, Kelliane A.
Sallet, Lunalva A. P.
Campos, Pollyanna F.
Prates, Maura V.
Silva, Luciano P.
collection Education Resources Information Center
contents Partial Characterization of a Novel Amphibian Hemoglobin as a Model for Graduate Student Investigation on Peptide Chemistry, Mass Spectrometry, and Atomic Force Microscopy Bemquerer, Marcelo P. Macedo, Jessica K. A. Ribeiro, Ana Carolina J. Carvalho, Andrea C. Silva, Debora O. C. Braz, Juliana M. Medeiros, Kelliane A. Sallet, Lunalva A. P. Campos, Pollyanna F. Prates, Maura V. Silva, Luciano P. Chemistry Graduate Students Science Instruction College Science Spectroscopy Nuclear Energy Biology Biomedicine Scientific Concepts Cytology Laboratory Equipment Science Process Skills Graduate students in chemistry, and in biological and biomedical fields must learn the fundamentals and practices of peptide and protein chemistry as early as possible. A project-oriented approach was conducted by first-year M.Sc and Ph.D students in biological sciences. A blind glass slide containing a cellular smear and an aqueous cellular extract were offered to the students. Qualitative and quantitative cell morphological parameters were analyzed by atomic force microscopy. The fractionation of the aqueous extract was conducted by reversed-phase chromatography followed by analysis of the isolated and partially purified proteins and peptides by mass spectrometry (MS). The proteins were treated by peptidases and the obtained peptide fragments were sequenced by "de novo" MS/MS, together with peptides already present in the extract. The most abundant protein fractions were identified as the alpha and beta chains of hemoglobin from an amphibian of the "Leptodactylus" genera. Two of the peptides sequenced by the students were synthesized by the solid-phase methodology, one of those being obtained by the split-and-pool library synthesis method. Thus, the students were able to learn some advanced principles and practices of protein chemistry and bionanotechnology in a 6-weeks project-oriented approach. (Contains 4 figures, 1 table and 4 notes.)
format Recurso educativo Open Access
id eric_EJ990932
institution ERIC Institute of Education Sciences
language en
publishDate 2012
record_format eric
spellingShingle Partial Characterization of a Novel Amphibian Hemoglobin as a Model for Graduate Student Investigation on Peptide Chemistry, Mass Spectrometry, and Atomic Force Microscopy
Bemquerer, Marcelo P.
Macedo, Jessica K. A.
Ribeiro, Ana Carolina J.
Carvalho, Andrea C.
Silva, Debora O. C.
Braz, Juliana M.
Medeiros, Kelliane A.
Sallet, Lunalva A. P.
Campos, Pollyanna F.
Prates, Maura V.
Silva, Luciano P.
Chemistry
Graduate Students
Science Instruction
College Science
Spectroscopy
Nuclear Energy
Biology
Biomedicine
Scientific Concepts
Cytology
Laboratory Equipment
Science Process Skills
Partial Characterization of a Novel Amphibian Hemoglobin as a Model for Graduate Student Investigation on Peptide Chemistry, Mass Spectrometry, and Atomic Force Microscopy Bemquerer, Marcelo P. Macedo, Jessica K. A. Ribeiro, Ana Carolina J. Carvalho, Andrea C. Silva, Debora O. C. Braz, Juliana M. Medeiros, Kelliane A. Sallet, Lunalva A. P. Campos, Pollyanna F. Prates, Maura V. Silva, Luciano P. Chemistry Graduate Students Science Instruction College Science Spectroscopy Nuclear Energy Biology Biomedicine Scientific Concepts Cytology Laboratory Equipment Science Process Skills Graduate students in chemistry, and in biological and biomedical fields must learn the fundamentals and practices of peptide and protein chemistry as early as possible. A project-oriented approach was conducted by first-year M.Sc and Ph.D students in biological sciences. A blind glass slide containing a cellular smear and an aqueous cellular extract were offered to the students. Qualitative and quantitative cell morphological parameters were analyzed by atomic force microscopy. The fractionation of the aqueous extract was conducted by reversed-phase chromatography followed by analysis of the isolated and partially purified proteins and peptides by mass spectrometry (MS). The proteins were treated by peptidases and the obtained peptide fragments were sequenced by "de novo" MS/MS, together with peptides already present in the extract. The most abundant protein fractions were identified as the alpha and beta chains of hemoglobin from an amphibian of the "Leptodactylus" genera. Two of the peptides sequenced by the students were synthesized by the solid-phase methodology, one of those being obtained by the split-and-pool library synthesis method. Thus, the students were able to learn some advanced principles and practices of protein chemistry and bionanotechnology in a 6-weeks project-oriented approach. (Contains 4 figures, 1 table and 4 notes.)
title Partial Characterization of a Novel Amphibian Hemoglobin as a Model for Graduate Student Investigation on Peptide Chemistry, Mass Spectrometry, and Atomic Force Microscopy
topic Chemistry
Graduate Students
Science Instruction
College Science
Spectroscopy
Nuclear Energy
Biology
Biomedicine
Scientific Concepts
Cytology
Laboratory Equipment
Science Process Skills
url https://eric.ed.gov/?id=EJ990932