CONFERENCE SERIES: Drug & Device Safety
Recorded at: PepTalk: The Protein Science Week
Digital Course: Dynamic Light Scattering Theory, Do's & Don'ts, and Data Interpretation
About this Product:
Since its market introduction circa 30 years back, dynamic light scattering (DLS) has occupied a position of increasing popularity within the area of protein aggregate detection and characterization, due in large part to the non-invasiveness of the technique, the minimal sample volume & concentration requirements, and the quickness of data collection. While modern instrument design and software have removed much of the mystic traditionally associated with the technique, data interpretation is still an area of frustration for many DLS users. This digital course covers the basic theory behind DLS instrumentation, with a focus on the do's & don'ts when it comes to data interpretation.
Rational Design of Protein Solutions
Thomas M. Laue, Ph.D.
Nick Pace, Ph.D.
About this Product:
Over 197 Slides
Individual Copy: $345
Site License: $1380
Agenda At A Glance:
Since its market introduction circa 30 years back, dynamic light scattering (DLS) has occupied a position of increasing popularity within the area of protein aggregate detection and characterization, due in large part to the non-invasiveness of the technique, the minimal sample volume & concentration requirements, and the quickness of data collection. While modern instrument design and software have removed much of the mystic traditionally associated with the technique, data interpretation is still an area of frustration for many DLS users. This workshop covers the basic theory behind DLS instrumentation, with a focus on the do's & don'ts when it comes to data interpretation.
Part 1: DLS Theory & Data Interpretation
Part 2: Working DLS Examples
Dr Mattison completed his doctorate in biological chemistry at Purdue University, where he studied the effects of polyelectrolyte additives on the stability and activity of transport proteins and enzymes. From there he joined Protein Solutions as the Applications Development and Technical Support Manager, and was instrumental in helping to drive the adoption of sub-micron light scattering techniques from esoteric technologies into main stream laboratory tools. In 2002 Dr. Mattison joined Malvern Instruments, where he served as Applications Manager, Product Manager, and Director of Customer Support, prior to assuming his current position as Principal Scientist – Bioanalytics in the Strategic Technology Development Group.
Dr. Ulf Nobbmann received his Ph.D. in colloidal physics from Oklahoma State University, where he investigated the scattering of light from micron & sub-micron sized particle systems under both dilute and concentration conditions. Upon graduation, he joined Protein Solutions, where he turned his attention to the application of colloidal principles and characterization techniques to biological molecules and nano particles. Dr. Nobbmann has written two book chapters and numerous articles. He joined Malvern Instruments in 2003, where he served as Product Manager for their multi-angle light scattering systems prior to assuming his current role as the Senior Applications Specialist for the Nanometrics group of sub-micron particle characterization technologies at Malvern Instruments.
Jean-Luc Brousseau, Ph.D.
Dr. Jean-Luc Brousseau received his Ph.D. in Biophysics from the Universite du Quebec a Trois-Rivieres in 1999. His Ph.D. research was conducted at the University of Miami on macromolecules and sol-gels. His Post Doctoral research at Tulane University was on light scattering of polymer and novel characterization of polymerization reaction. At Tulane Dr. Brousseau developed an online characterization technique for measuring polymerization reaction kinetics. He then joined Brookhaven Instruments as a development specialist designing and introducing many instruments. He worked as a senior scientist at Brookhaven for 5 years on light scattering of proteins and polymers. Dr. Brousseau joined Malvern Instrument in 2007 where he was a Development Specialist for the flow-mode absolute size exclusion chromatography (ASEC) for the Zetasizer Nano light scattering instrument. He is now in the separation division working with the Viscotek line of instruments.
This digital course includes two bonus presentations including: "Overview on Colloidal Versus Molecular Solution Stability" delivered by Thomas M. Laue, Ph.D., Professor, Biochemistry and Molecular Biology; Director, Biomolecular Interaction Technologies Center (BITC), University of New Hampshire and “Increasing Protein Stability and Solubility” delivered by C. Nick Pace, Ph.D., Professor, Medical Biochemistry and Genetics and of Biochemistry and Biophysics, Texas A&M. These two talks were part of the course on Rational Design of Protein Solutions, which was also a part of PepTalk.
Overview on Colloidal Versus Molecular Solution Stability
Thomas M. Laue, Ph.D., Professor, Biochemistry and Molecular Biology; Director, Biomolecular Interaction Technologies Center (BITC), University of New Hampshire
Tom Laue is the Capenter Professor of Molecular, Cellular and Biomedical Sciences, and professor of Material Sciences at the University of New Hampshire. He is the Director of both the Center to Advance Molecular Interaction Science and the Biomolecular Interaction Technologies Center.
He received his bachelor’s degree in Natural Sciences from the Johns Hopkins University in 1971and his Ph.D. in Biophysics and Biochemistry from the University of Connecticut in 1981. His post-doctoral studies were conducted at the University of Oklahoma. Between 1969 and 1975, he worked as a technician in the deep space program of NASA.
He joined the University of New Hampshire in 1984 as an Assistant Professor, and teaches both undergraduate and graduate courses in biochemistry and biophysics. His research focuses on the development of instrumentation and methods that use the fundamental properties of mass and charge for examining macromolecular interactions. His instruments can provide unique insights into these interactions, which has resulted in extensive collaborations with both academic and industrial labs. Tom has over 120 publications, serves on several editorial boards, and gives over one hundred lectures, seminars and workshops a year.
Increasing Protein Stability and Solubility
C. Nick Pace, Ph.D., Professor, Medical Biochemistry and Genetics and of Biochemistry and Biophysics, Texas A&M
Dr. Nick Pace received his B.S. in Chemistry from the University of Utah in 1962, and his Ph.D. in Biochemistry from Duke University in 1966 working with Dr. Charles Tanford. His postdoctoral work was in the Chemistry Dept. at Cornell University working with Dr. Gordon Hammes. He joined the faculty at Texas A&M in 1968. In 1982 he took a Sabbatical at the MRC Centre in Cambridge England working with Dr. Tom Creighton and Dr. Alan Barrett. In 1992 he was a Visiting Professor at Osaka University in the Institute for Protein Research.
The important tasks in living cells are carried out by proteins in which the polypeptide chain is folded into a globular structure that is essential for their biological function. The amino acid sequence of the protein determines the folded structure. Proteins can now be constructed with any desired amino acid sequence. The potential applications of this technology in health and other areas are limited only by our knowledge and imagination. We try to learn how changes in the amino acid sequence effect the structure, function, solubility, and stability of a protein. Our ultimate goal is to be able to predict the folded structure of a protein given just the amino acid sequence.
About the Conference:
CHI’s 10th Annual PepTalk event features strong scientific programming comprising fourteen conferences within topic focused pipelines. The four distinct pipelines range from applying protein discovery research, to developing downstream protein expression, characterization, formulation, and production that ultimately leads to clinical applications. This event is designed with you in mind. Stay within a specific pipeline or track hop, and create a custom agenda to meet your research and networking needs.