Event Title

How Sequence Directs Structure: My First Steps to Unlock the Protein Folding Code in GB1

Student Presenter Information

Brittney Ruedlinger, Old Dominion University

Presentation Type

Event

Description/Abstract

The β1 domain of Streptococcal protein G consists of 56 amino acid residues arranged in a two-layer alpha-beta sandwich. We are interested in understanding how the sequence encodes the three-dimensional structure of this protein. In support of this research investigation, two mutations were selected, designed and synthesized. The first is glutamic acid 42 to glycine and the second is valine 39 to alanine. The variant proteins were expressed in preparation for future experimental studies which will involve purifying the proteins as well as conducting thermodynamic and kinetic studies to elucidate the effect of the mutations on structure, stability and folding.

Comments

Faculty Mentor: Dr. Lesley Greene

Chemistry and Biochemistry

Location

Learning Commons @ Perry Library, Northwest Atrium

Start Date

13-2-2016 8:00 AM

End Date

13-2-2016 12:30 PM

Full Text of Presentation

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Feb 13th, 8:00 AM Feb 13th, 12:30 PM

How Sequence Directs Structure: My First Steps to Unlock the Protein Folding Code in GB1

Learning Commons @ Perry Library, Northwest Atrium

The β1 domain of Streptococcal protein G consists of 56 amino acid residues arranged in a two-layer alpha-beta sandwich. We are interested in understanding how the sequence encodes the three-dimensional structure of this protein. In support of this research investigation, two mutations were selected, designed and synthesized. The first is glutamic acid 42 to glycine and the second is valine 39 to alanine. The variant proteins were expressed in preparation for future experimental studies which will involve purifying the proteins as well as conducting thermodynamic and kinetic studies to elucidate the effect of the mutations on structure, stability and folding.