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Lecture

The Biochemistry of Fear and Organic Chemistry Concepts

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 biochemistry of fear, focusing on the brain regions involved in the fear response and the neurotransmitters responsible for it. Additionally, it delves into organic chemistry concepts such as resonance structures, acidity, and base stabilization by inductive effects.

Instructors (7)

Beat Fierz

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.

Jérôme Waser

Jérôme Waser biography and CV's are available on the following website: http://lcso.epfl.ch/waser

Angela Steinauer

Marinella Mazzanti

Official source

Related concepts (32)

Resonance

Resonance describes the phenomenon of increased amplitude that occurs when the frequency of an applied periodic force (or a Fourier component of it) is equal or close to a natural frequency of the system on which it acts. When an oscillating force is applied at a resonant frequency of a dynamic system, the system will oscillate at a higher amplitude than when the same force is applied at other, non-resonant frequencies. Frequencies at which the response amplitude is a relative maximum are also known as resonant frequencies or resonance frequencies of the system.

Acid

An acid is a molecule or ion capable of either donating a proton (i.e. hydrogen ion, H+), known as a Brønsted–Lowry acid, or forming a covalent bond with an electron pair, known as a Lewis acid. The first category of acids are the proton donors, or Brønsted–Lowry acids. In the special case of aqueous solutions, proton donors form the hydronium ion H3O+ and are known as Arrhenius acids. Brønsted and Lowry generalized the Arrhenius theory to include non-aqueous solvents.

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.

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