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Lecture

Protein Folding: Forces and Mechanisms

In course

PHYS-468: Physics of life

Life has emerged on our planet from physical principles such as molecular self-organization, thermodynamics, stochastics and iterative refinement. This course will introduce the physical methods to study life and will discuss the quantitative and physical ...

Description

This lecture delves into the intricate process of protein folding, exploring the key forces involved such as van der Waals interactions, the hydrophobic effect, hydrogen bonds, and salt bridges. It also discusses the destabilizing factors like chain entropy and bond strain, providing insights into the complex interplay of stabilizing and destabilizing forces. The lecture further covers the estimation of net magnitudes of these forces in protein folding and the thermal melting of proteins. Additionally, it examines the applications of ThermoFluor in studying protein stability and ligand binding, shedding light on how ligand binding can stabilize protein structures.

Instructor

Henning Paul-Julius Stahlberg

Positions: Since 2020 Prof. Physics, IPHYS, SB, EPFL, Switzerland 2009 – 2021 Prof. Structural Biology, Biozentrum, University Basel, Switzerland 2009 – 2010 Adj. Assoc. Prof. Molecular & Cellular Biology, UC Davis, CA, USA 2007 – 2009 Assoc. Prof. Molecular & Cellular Biology, UC Davis, CA, USA 2003 – 2007 Assist. Prof. Molecular & Cellular Biology, UC Davis, CA, USA Education: 2002 Habilitation, Biozentrum, University Basel, Switzerland 1997 – 2003 Postdoctoral Fellow, Biozentrum, University Basel, Switzerland 1992 – 1997 PhD Student, EPFL, Lausanne, Switzerland 1990 – 1991 Diploma Thesis in Solid State Physics, TU Berlin, Germany 1987 – 1993 Study of Physics, TU Berlin, Germany Selected Awards & Honors: 2009 W.M.Keck Award 2004 CAREER award, NSF, USA 2002 Habilitation, University Basel, Switzerland Selected Memberships: 2008 – 2013 Chancellor’s Fellow Award, UC Davis, CA, USA 2004 – 2009 Faculty of 1000 Since 1992 Swiss Society for Optics and Microscopy (SSOM)

Official source

Related concepts (32)

Protein folding

Protein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.

Hydrogen bond

In chemistry, a hydrogen bond (or H-bond) is a primarily electrostatic force of attraction between a hydrogen (H) atom which is covalently bound to a more electronegative "donor" atom or group (Dn), and another electronegative atom bearing a lone pair of electrons—the hydrogen bond acceptor (Ac). Such an interacting system is generally denoted , where the solid line denotes a polar covalent bond, and the dotted or dashed line indicates the hydrogen bond.

Van der Waals force

In molecular physics, the van der Waals force is a distance-dependent interaction between atoms or molecules. Unlike ionic or covalent bonds, these attractions do not result from a chemical electronic bond; they are comparatively weak and therefore more susceptible to disturbance. The van der Waals force quickly vanishes at longer distances between interacting molecules. Named after Dutch physicist Johannes Diderik van der Waals, the van der Waals force plays a fundamental role in fields as diverse as supramolecular chemistry, structural biology, polymer science, nanotechnology, surface science, and condensed matter physics.

Ligand (biochemistry)

In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. The etymology stems from Latin ligare, which means 'to bind'. In protein-ligand binding, the ligand is usually a molecule which produces a signal by binding to a site on a target protein. The binding typically results in a change of conformational isomerism (conformation) of the target protein. In DNA-ligand binding studies, the ligand can be a small molecule, ion, or protein which binds to the DNA double helix.

Ring strain

In organic chemistry, ring strain is a type of instability that exists when bonds in a molecule form angles that are abnormal. Strain is most commonly discussed for small rings such as cyclopropanes and cyclobutanes, whose internal angles are substantially smaller than the idealized value of approximately 109°. Because of their high strain, the heat of combustion for these small rings is elevated. Ring strain results from a combination of angle strain, conformational strain or Pitzer strain (torsional eclipsing interactions), and transannular strain, also known as van der Waals strain or Prelog strain.

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