Lecture

Organic Chemistry: Delocalization and Resonance Structures

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In course

CH-110: Advanced general chemistry I

Le cours comporte deux parties. Les bases de la thermodynamique des équilibres et de la cinétique des réactions sont introduites dans l'une d'elles. Les premières notions de chimie quantique sur les électrons et les liaisons chimiques, exemplifiées en chim ...

Description

This lecture explores the importance of organic chemistry in everyday compounds, focusing on the biochemistry of fear and the regions of the brain involved in the fear response. It delves into the concept of resonance structures, discussing factors affecting stability, isomers versus resonance structures, and the generation and analysis of resonance structures. The lecture also covers the relative importance of resonance structures, electron delocalization in cyclic molecules, and the significance of resonance in understanding reactivity. Additionally, it addresses the role of resonance in aromatic compounds, the impact of double bonds on resonant structures, and the relationship between resonance structures and acidity.

Instructors (7)

Philippe Schwaller

Beat Fierz

Teaching & PhD PhD Students Paria Khalafi, Wei Cai, Pierre Alexander Miranda Herrera, Andrei Zhauniarovich, Matteo Nicolas Doudin, Zongqing Li, Enguerran Majerus, Po-Han Chang, Iana Berlina, Yuji Kamei Past EPFL PhD Students Aurore Marie-France Delachat, Sinan Kilic, Louise Catherine Bryan, Andreas Linus Bachmann, Ninad Dilip Agashe, Nora Guidotti, Maxime Nicolas Mivelaz, Kristina Makasheva, Alexandra Teslenko, Pauline Franz, Salome Riccarda Püntener, Ly Phillippe Past EPFL PhD Students as codirector Dani

Angela Steinauer

Since 2022: Head of the Laboratory of Biomolecular Engineering and Nanomedicine (LIBN), EPFL (Switzerland)2019-2021: MSCA Postdoctoral Fellow at ETHZ (Switzerland)2018: Ph.D. in Chemical Biology from Yale University (USA)2007-2012: B.Sc. & M.Sc. in Chemistry from University of Zurich (Switzerland) Teaching & PhD PhD Students Diogo Miguel De Abreu Viegas, Georges Barnikol, Oliver Dennis, Andrea Elizabeth Melgar Aguilar, Paula Oeser, Manutsawee Thanaburakorn Courses Advanced general chemistry I CH

Jacques-Edouard Moser

Jacques-Edouard Moser is titular professor in physical chemistry and is currently directing the Group for Photochemical Dynamics (Moser Group) of EPFL. He is a graduate of the École polytechnique fédérale de Lausanne, where he received a diploma degree (MSc) in chemical engineering in 1982. After two stays in 1984 and 1985 at Concordia University in Montréal (Canada), he earned in 1986 his Ph.D. in physical chemistry at EPFL (Michael Grätzel, thesis advisor). In 1986, he joined the Eastman Kodak Corporate Research Laboratories at Rochester (NY, USA) as a postdoctoral fellow and was later associated with the NSF Center for Photoinduced Electron Transfer at the University of Rochester. Returning to Switzerland, he was appointed as a lecturer of physical chemistry at EPFL in 1992 and was awarded the habilitation and the venia legendi in 1998. He is titular professor since 2005.His research activity focuses on the study of the dynamics of photoinduced electron transfer and charge carrier separation at donor-acceptor heterojunctions and in nanostructured semiconductors. He is the author and co-author of ca 200 scientific papers (H-index 75). He currently teaches general physical chemistry to freshmen students in chemistry. He gives two classes on general- and redox photochemistry in the MSc program in chemistry and chemical engineering and the doctoral programs in energy and photonics. Jacques-E. Moser presided the Swiss Society of Photochemistry and Photophysics (1995-1998) and chaired the jury of the Grammaticakis-Neumann international prize in photochemistry (1999-2001). He was a member of the board of the Swiss Chemical Society (2007-2012). He served as a member of the standing committee of the European Photochemistry Association (1992-2000) and of the executive committee of the division for fundamental research of the Swiss Chemical Society (1999-2014). He was the director of the Section of Chemistry and Chemical Engineering of EPFL and a member of the direction of the School of Basic Sciences from 2007 to 2015.

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Related concepts (32)

Resonance (chemistry)

In chemistry, resonance, also called mesomerism, is a way of describing bonding in certain molecules or polyatomic ions by the combination of several contributing structures (or forms, also variously known as resonance structures or canonical structures) into a resonance hybrid (or hybrid structure) in valence bond theory. It has particular value for analyzing delocalized electrons where the bonding cannot be expressed by one single Lewis structure.

Nuclear magnetic resonance spectroscopy

Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy or magnetic resonance spectroscopy (MRS), is a spectroscopic technique to observe local magnetic fields around atomic nuclei. This spectroscopy is based on the measurement of absorption of electromagnetic radiations in the radio frequency region from roughly 4 to 900 MHz. Absorption of radio waves in the presence of magnetic field is accompanied by a special type of nuclear transition, and for this reason, such type of spectroscopy is known as Nuclear Magnetic Resonance Spectroscopy.

Electron paramagnetic resonance

Electron paramagnetic resonance (EPR) or electron spin resonance (ESR) spectroscopy is a method for studying materials that have unpaired electrons. The basic concepts of EPR are analogous to those of nuclear magnetic resonance (NMR), but the spins excited are those of the electrons instead of the atomic nuclei. EPR spectroscopy is particularly useful for studying metal complexes and organic radicals. EPR was first observed in Kazan State University by Soviet physicist Yevgeny Zavoisky in 1944, and was developed independently at the same time by Brebis Bleaney at the University of Oxford.

Nuclear magnetic resonance spectroscopy of proteins

Nuclear magnetic resonance spectroscopy of proteins (usually abbreviated protein NMR) is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucleic acids, and their complexes. The field was pioneered by Richard R. Ernst and Kurt Wüthrich at the ETH, and by Ad Bax, Marius Clore, Angela Gronenborn at the NIH, and Gerhard Wagner at Harvard University, among others.

Nuclear magnetic resonance

Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a strong constant magnetic field are perturbed by a weak oscillating magnetic field (in the near field) and respond by producing an electromagnetic signal with a frequency characteristic of the magnetic field at the nucleus. This process occurs near resonance, when the oscillation frequency matches the intrinsic frequency of the nuclei, which depends on the strength of the static magnetic field, the chemical environment, and the magnetic properties of the isotope involved; in practical applications with static magnetic fields up to ca.

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