Prerequisites: Organic chemistry and biology courses, neuroscience or neurobiology recommended, but not required. The study of the brain is one of the most exciting frontiers in science and medicine today. Although neuroscience is by nature a multi-disciplinary effort, chemistry has played many critical roles in the development of modern neuroscience, neuropharmacology, and brain imaging. Chemistry, and the chemical probes it generates, such as molecular modulators, therapeutics, imaging agents, sensors, or actuators, will continue to impact neuroscience on both preclinical and clinical levels. In this course, two major themes will be discussed. In the first one, titled Imaging brain function with chemical tools, we will discuss molecular designs and functional parameters of widely used fluorescent sensors in neuroscience (calcium, voltage, and neurotransmitter sensors), their impact on neuroscience, pros and cons of genetically encoded sensors versus chemical probes, and translatability of these approaches to the human brain. In the second major theme, titled Perturbation of the brain function with chemical tools, we will examine psychoactive substances, the basics of medicinal chemistry, brain receptor activation mechanisms and coupled signaling pathways, and their effects on circuit and brain function. We will also discuss recent approaches, failures and successes in the treatment of neurodegenerative and psychiatric disorders. Recent advances in precise brain function perturbation by light (optogenetics and photopharmacology) will also be introduced. In the context of both themes we will discuss the current and future possibilities for the design of novel materials, drawing on the wide molecular structural space (small molecules, proteins, polymers, nanomaterials), aimed at monitoring, modulating, and repairing human brain function. This course is intended for students (undergraduate and graduate) from the science, engineering and medical departments.
The use of multinuclear NMR spectroscopy in the determination of the structures of inorganic molecules and the use of dynamic NMR spectroscopy (variable temperature NMR and magnetization transfer techniques) to provide information concerned with reaction mechanisms.
Prerequisites: elementary organic chemistry. Introduction to theory and practice of NMR spectroscopy. Instrumental aspects, basic NMR theory, NOE, and a survey of 2D methods are covered.
The goal of this course is to explore how chemical methods and concepts have impacted our ability to understand and manipulate protein structure and function. We will navigate this subject through a combination of lectures and structured discussions on research articles from the literature. The course is divided into three segments: (1) In the first part, we will review the rudiments of protein structure and function, then delve into various aspects of enzyme chemistry and polypeptide biosynthesis. (2) In the second part of the course, we will cover synthetic methods to produce and chemically modify peptides and proteins. (3) In the final part, we will discuss chemical approaches to control protein function and monitor protein activity, focusing on methods that use small molecules and mass spectrometry proteomics.
Prerequisites: CHEM UN2443 , or the equivalent.
This class will describe the electronic and physical structure of inorganic materials with an emphasis on colloidal quantum dots and surface science.
Main group and transition metal organometallic chemistry: bonding, structure, reactions, kinetics, and mechanisms.
The only prerequisites needed include General Chemistry II Lectures (specifically, kinetics, and at the level of UN1404 or UN1604) and Organic Chemistry II Lectures (at the level of UN2046 or UN2444). Advanced knowledge from classes, including but not limited to physical chemistry, inorganic chemistry, advanced organic chemistry, and synthetic methods, is NOT required.
Departments permission.