PepTalk 2017
PepTalk 2017

Membrane Proteins header

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Conference Short Courses*View Details 

Sunday, January 9 - 3:00 pm - 6:00 pm

  • Protein Crystallization - Delineating Protein Structure
  • DoE and QbD: Tools for Optimizing the Bioprocess

Thursday, January 13 - 6:30 pm - 9:00 pm

  • Rational Design of Protein Solutions


This meeting addresses the insoluble nature of membrane proteins, their function and interrelationships, the challenges of achieving scale, and their importance as drug targets. 
Along the way, we will discover how membrane proteins are housed – either fully or partially – in lipid bilayers, and why they are considered to be extremely important intermediaries.  For researchers who are familiar with soluble proteins, Membrane Proteins’ hydrophobic nature poses a significant barrier to extraction and keeping them stable in an aqueous state.  Key leaders who have successfully accomplished this feat share their insights and protocols for expression and purification.


1:00pm  Conference Registration


Delineating Structure, Function and Interactions

1:45  Chairperson’s Opening Remarks

Helen Zgurskaya, Ph.D., Professor, Chemistry and Biochemistry, University of Oklahoma

1:50  Opening Keynote Presentation:
Membrane Proteins in the Service of Human Health

Robert StroudRobert Stroud, Ph.D., Professor, Biochemistry & Biophysics; Pharmaceutical Chemistry, University of California, San Francisco

Integral membrane proteins account for ~30% of a proteome and play critical roles in metabolic, regulatory and intercellular processes. Human MPs are the targets for ~40% of all therapeutic drugs, but the number of MP structures is less than 0.5% of the number of soluble protein structures. The presentation addresses the key issues that need to be addressed to obtain pure, functional, homogeneous, stable membrane proteins, lessons and methods that are advancing this key area of membrane biology in the service of human health.

2:20  Structural Study of a Membrane Protein in a Lipid Membrane by Cryo-EM

Liguo Wang, Ph.D., Associate Research Scientist, Yale School of Medicine

Structural study of membrane proteins has been hampered by the difficulty in forming crystals for X-ray or electron crystallography. Here, we report a novel and general method to study membrane proteins in their native lipid membrane environments using electron cryo-microscopy (cryo-EM). This new method is called random spherically constrained single-particle reconstruction, which allows the structure determination of membrane proteins reconstituted into small, spherical liposomes. We have successfully employed this new method to obtain the structure of a 500 kDa ion channel complex, the BK calcium-activated potassium channel.

2:50  Tryptophan-Lipid Interactions in Membrane Protein Folding

Judy Kim, Ph.D., Assistant Professor, Chemistry and Biochemistry, University of California, San Diego

The research in our group focuses on specific protein-lipid interactions that are critical for stability and folding of membrane proteins and peptides. We utilize a technique that provides structural information and therefore, is capable of revealing molecular details that are unobtainable by typical biophysical tools such as fluorescence and circular dichroism. We have probed protein-lipid interactions of integral membrane proteins as well as membrane-associated peptides, including the toxins and antimicrobial peptides.

Sponsored by
3:20  Screening of Membrane Proteins using Profinia Prior to Large-Scale Purification

Said Eshaghi, Ph.D., Associate Professor, Biomedical Structural Biology, School of Biological Sciences, Nanyang Technological University, Singapore
Producing large amount of homogeneous and stable protein is one of the major hurdles in structural biology of integral membrane proteins. Identification of the optimal parameters, such as detergent and ionic strength is the necessary step prior to large-scale membrane protein purification. Thus, it is important to use a strategy that is both scalable as well as cost-efficient, due to high detergent cost. This talk will focus on the strategies we use to screen for identifying optimum conditions for membrane protein production, including the usage of Profinia protein purification system. The latter will offer a cost-efficient, robust and scalable strategy.

3:35  Refreshment Break, Exhibit and Poster Viewing


Overcoming Challenges

4:30  Elucidating the Structure and Function of Membrane Proteins through Nanotechnology

Stephen G. Sligar, Ph.D., I.C. Gunsalus Professor, Director, School of Molecular and Cellular Biology, Center for Biophysics and Computational Biology, College of Medicine, University of Illinois at Urbana-Champaign

Nanodiscs are soluble nanoscale phospholipid bilayers which can self-assemble integral membrane proteins for subsequent biophysical, enzymatic and structural investigations. Rendering membrane proteins soluble at the single molecule level offers advantages over liposomes or detergent micelles in terms of size, stability, ability to add genetically modifiable features to the Nanodisc structure, control of oligomerization and ready access to both sides of the phospholipid bilayer domain. In my lecture I will provide an overview of the Nanodisc approach and document several recent applications in the structural and functional investigation of membrane proteins.

5:00  Using the Nanodisc to Study Membrane Protein Structure and Dynamics: Three Case Studies

Franck Duong, Ph.D., Associate Professor, Biochemistry, The University of British Columbia

We are challenging the difficulties inherent with membrane proteins by applying the phospholipid/protein nanostructures, or Nanodiscs. Due to their homogeneity, solubility and stability, these lipoparticles allow us to perform experiments with unprecedented control over the lipid environment and membrane protein composition. We have developed this novel vector on three selected model protein systems, to provide novel insights in the fields of membrane biology and lipoprotein engineering.

5:30  Membrane Proteomics of Cancer Cells

Shen Hu, Ph.D., Assistant Professor, UCLA School of Dentistry and Jonsson Comprehensive Cancer Center, UCLA

Membrane proteins play a critical role in cancer cell adhesion, migration and invasion. Membrane proteomics of cancer cells represents a valuable approach to understanding cancer cell biology and discovering target molecuels for disease applications. We have profiled membrane proteins in pancreatic and oral cancer cells using mass spectrometry-based proteomics. Further validation study and siRNA-based functional analysis suggested membrane proteins are involved in growth and metastasis of cancer cells. These proteins may serve as biomarkers for cancer detection or novel targets for therapeutic intervention.

6:00 Close of Day

Day 1 | Day 2 | Download Brochure 

Links to Companion Meetings

Pipeline 1

Targeting Genes, Engineering Vectors, Designing Constructs and Optimizing Clones 

Choosing, Designing, and Optimizing Hosts and Platforms 

Overcoming Protein Expression Challenges with Solutions