The Art of Changing the Brain: Enriching the Practice of Teaching by Exploring the Biology of Learning

“Engaging and logically organized…Readers will feel encouraged and eager to integrate the concepts into their own philosophy of teaching and learning. ?Effective Teaching The book is not merely an explication but a thoughtfully crafted, neuroscientfically informed teaching device that obeys the advice offered. ?American Journal of Psychology James Zull\u27s crystal-clear mapping of how learning occurs, how learning changes the brain, and how many parts of the brain are activated as one learns should be interesting for all who teach. Zull relays a teaching approach and the neuroscience behind that approach that can dramatically affect learning. ?Nursing Education Perspectives This is the best book I have read about the brain and learning. Zull perspective forms the foundation for a teaching approach that can dramatically improve human learning. ?David A. Kolb, Dept. of Organizational Behavior, Case Western Reserve UniversityJames Zull invites teachers in higher education or any other setting to accompany him in his exploration of what scientists can tell us about the brain and to discover how this knowledge can influence the practice of teaching. He describes the brain in clear non-technical language and an engaging conversational tone, highlighting its functions and parts and how they interact, and always relating them to the real world of the classroom and his own evolution as a teacher

Effect Of Methionine Oxidation And Deletion Of Amino-Terminal Residues On The Conformation Of Parathyroid Hormone. Circular Dichroism Studies.

Circular dichroism (CD) studies of parathyroid hormone (PTH), its oxidized forms, and some fragments of the hormone are described. The CD spectrum of native PTH (84 amino acids) and the active fragment, 1-34 PTH, suggests that most of the secondary structure resides in the amino-terminal segment of this hormone. Oxidation of the methionine residue at position 18 has a small impact on secondary structure, whereas oxidation of the methionine at position 8 produces substantial changes. Oxidation of both methionines produces secondary structure changes that are greater than the sum of those seen upon oxidation of the individual methionines. The CD spectrum for the 3-34 fragment of PTH is identical to that of the 1-34 fragment, and that of the 7-34 fragment is only slightly different. The spectra of the 13-34 and 19-34 fragments are markedly altered from that of the 1-34 peptide, and those of the 9-84 and 19-84 fragments of native PTH are significantly different from the intact hormone. Computer-assisted estimates of secondary structure content, and difference spectra, were utilized to evaluate the secondary structure content of the peptides. These results suggest that residues 6-12 are important in formation of helical secondary structure and that a reverse turn may be important for the folding of PTH into a conformation with high affinity for receptors. Residues 1 and 2 appear to make no contribution to the secondary structure and may be directly involved in activation of receptors