Lecture

Protein Folding: Thermodynamic Insights

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In course

BIO-212: Biological chemistry I

Biochemistry is a key discipline for the Life Sciences. Biological Chemistry I and II are two tightly interconnected courses that aim to describe and understand in molecular terms the processes that make life possible. ...

Description

This lecture covers the energetic determinants of protein folding, protein-protein interactions, and the concept of free energy. It discusses the importance of enthalpy, entropy, and heat capacity in protein folding, as well as equilibrium constants and examples like ATP hydrolysis and acid-base equilibrium. The lecture also explores the thermodynamic properties of proteins, focusing on unfolding reactions, melting temperature, and the measurement of enthalpy and entropy. Through examples and concepts like the hydrophobic effect, students learn how to compute pkas for residues within the protein environment.

Instructors (4)

Matteo Dal Peraro

Matteo Dal Peraro graduated in Physics at the University of Padua in 2000. He obtained his Ph.D. in Biophysics at the International School for Advanced Studies (SISSA, Trieste) in 2004. He then received postdoctoral training at the University of Pennsylvania (Philadelphia) under the guidance of Prof. M. L. Klein. He was nominated Tenure Track Assistant Professor at the EPFL School of Life Sciences in late 2007. His research at the Laboratory for Biomolecular Modeling (LBM), within the Interfaculty Institute of Bioengineering (IBI), focuses on the multiscale modeling of large macromolecular systems.

Bruno Emanuel Ferreira De Sousa Correia

Throughout my PhD and postdoctoral studies I was trained in world-renowned laboratories and institutions in the United States of America (University of Washington and The Scripps Research Institute). Very early in my scientific career I found out my fascination about protein structure and function. My PhD studies evolved in the direction of immunogen design and vaccine engineering which sparked my interest in the many needs and opportunities in vaccinology and translational research. My efforts resulted in an enlightening piece of work where for the first time, computationally designed immunogens elicited potent neutralizing antibodies. During my postdoctoral studies I joined a chemical biology laboratory at the Scripps Research Institute. In this stage I developed novel chemoproteomics methods for the identification of protein-small molecule interaction sites in complex proteomes. In March 2015, I joined the École Polytechnique Fédérale de Lausanne (EPFL) – Switzerland as a tenure track assistant professor. The focus of my research group is to develop computational tools for protein design with particular emphasis in applying these strategies to immunoengineering (e.g. vaccine and cancer immunotherapy). The activities in my laboratory focus on computational design methods development and experimental characterization of the designed proteins. Our laboratory has been awarded with 2 prestigious research grants from the European Research Council. Lastly, I have been awarded the prize for best teacher of Life sciences in 2019.

Giovanni D'Angelo

Teaching & PhD PhD Students Mélissa Ruiz, Gary Domeniconi, Irmak Kaysudu, Alessandro Valente, Surayyo Akramkhanova, Jean Andrea Maillat, Linda Wedemann, Manel Leila Nadia Boussouf, Jiayan Lin, Nika Gorsek, Christina Ulrich, William Daniel Chan-Ha Verdier Past EPFL PhD Students Laura Capolupo, Jaipreet Singh Loomba, Halima Hannah Emilie Schede Past EPFL PhD Students as codirector Muhammad Umair Anwar Courses Biological chemistry II BIO-213 Biochemistry is a key discipline in the Life Scienc

Official source

Ontological neighbourhood

Physics

Thermodynamics: Statistical mechanics

Related concepts (32)

Chemical equilibrium

In a chemical reaction, chemical equilibrium is the state in which both the reactants and products are present in concentrations which have no further tendency to change with time, so that there is no observable change in the properties of the system. This state results when the forward reaction proceeds at the same rate as the reverse reaction. The reaction rates of the forward and backward reactions are generally not zero, but they are equal. Thus, there are no net changes in the concentrations of the reactants and products.

Thermodynamics

Thermodynamics is a branch of physics that deals with heat, work, and temperature, and their relation to energy, entropy, and the physical properties of matter and radiation. The behavior of these quantities is governed by the four laws of thermodynamics which convey a quantitative description using measurable macroscopic physical quantities, but may be explained in terms of microscopic constituents by statistical mechanics.

Acid dissociation constant

In chemistry, an acid dissociation constant (also known as acidity constant, or acid-ionization constant; denoted K_a) is a quantitative measure of the strength of an acid in solution. It is the equilibrium constant for a chemical reaction HA A^- + H^+ known as dissociation in the context of acid–base reactions. The chemical species HA is an acid that dissociates into , the conjugate base of the acid and a hydrogen ion, .

Boltzmann distribution

In statistical mechanics and mathematics, a Boltzmann distribution (also called Gibbs distribution) is a probability distribution or probability measure that gives the probability that a system will be in a certain state as a function of that state's energy and the temperature of the system. The distribution is expressed in the form: where pi is the probability of the system being in state i, exp is the exponential function, εi is the energy of that state, and a constant kT of the distribution is the product of the Boltzmann constant k and thermodynamic temperature T.

Specific heat capacity

In thermodynamics, the specific heat capacity (symbol c) of a substance is the heat capacity of a sample of the substance divided by the mass of the sample, also sometimes referred to as massic heat capacity. Informally, it is the amount of heat that must be added to one unit of mass of the substance in order to cause an increase of one unit in temperature. The SI unit of specific heat capacity is joule per kelvin per kilogram, J⋅kg−1⋅K−1.

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