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Lecture

Characterization of Proteins by Electrophoresis

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 covers the physics behind the electrophoresis technique used for the characterization of proteins, including Native Gel, SDS-PAGE, and 2D Gel. It explains the different types of gels commonly used, the range of separation for DNA and proteins, and the stains used for biopolymers after electrophoretic separation. The lecture also delves into isotachophoresis within the stacking gel zone and the principles of SDS-PAGE in denaturing and non-denaturing conditions.

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

Ontological neighbourhood

Biology

Molecular biology: Topics in molecular biology

Related concepts (25)

Gel electrophoresis

Gel electrophoresis is a method for separation and analysis of biomacromolecules (DNA, RNA, proteins, etc.) and their fragments, based on their size and charge. It is used in clinical chemistry to separate proteins by charge or size (IEF agarose, essentially size independent) and in biochemistry and molecular biology to separate a mixed population of DNA and RNA fragments by length, to estimate the size of DNA and RNA fragments or to separate proteins by charge.

Polyacrylamide gel electrophoresis

Polyacrylamide gel electrophoresis (PAGE) is a technique widely used in biochemistry, forensic chemistry, genetics, molecular biology and biotechnology to separate biological macromolecules, usually proteins or nucleic acids, according to their electrophoretic mobility. Electrophoretic mobility is a function of the length, conformation, and charge of the molecule. Polyacrylamide gel electrophoresis is a powerful tool used to analyze RNA samples.

Agarose gel electrophoresis

Agarose gel electrophoresis is a method of gel electrophoresis used in biochemistry, molecular biology, genetics, and clinical chemistry to separate a mixed population of macromolecules such as DNA or proteins in a matrix of agarose, one of the two main components of agar. The proteins may be separated by charge and/or size (isoelectric focusing agarose electrophoresis is essentially size independent), and the DNA and RNA fragments by length.

Two-dimensional gel electrophoresis

Two-dimensional gel electrophoresis, abbreviated as 2-DE or 2-D electrophoresis, is a form of gel electrophoresis commonly used to analyze proteins. Mixtures of proteins are separated by two properties in two dimensions on 2D gels. 2-DE was first independently introduced by O'Farrell and Klose in 1975. 2-D electrophoresis begins with electrophoresis in the first dimension and then separates the molecules perpendicularly from the first to create an electropherogram in the second dimension.

Protein

Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity.

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