Title

Knob-Socket Mapping of a-Helical Proteins

Poster Number

29

Lead Author Major

Biochemistry

Format

Poster Presentation

Faculty Mentor Name

Jerry Tsai

Faculty Mentor Department

Chemistry

Additional Faculty Mentor Name

Hyun Joo

Abstract/Artist Statement

Current maps used for designing helical proteins are extremely limited in their ability to display the location of the proteins and inter- and intrahelical relationships between the proteins, thus making it difficult to design new proteins on paper. Here we present a new method of mapping out helical proteins: the Knob-Socket map. This new map lays out the entire protein helix on a 2-D map, displaying the bonding structure between the amino acids. The shading patterns displays the interaction between the separate helices. Using the Knob-Socket map, we can not only clearly map out proteins, but we can also study the effects the specific observed bonding patterns have on the proteins, where interactions might take place, as well as the folding patterns of the protein. As shown here, the α-helical coiled map shows interval clusters of knob-socket interactions, which is characteristic of the crossing-over of the helices. It is also possible to show the order in which the helices are in.

Location

DeRosa University Center, Ballroom

Start Date

30-4-2016 1:30 AM

End Date

30-4-2016 3:30 PM

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Apr 30th, 1:30 AM Apr 30th, 3:30 PM

Knob-Socket Mapping of a-Helical Proteins

DeRosa University Center, Ballroom

Current maps used for designing helical proteins are extremely limited in their ability to display the location of the proteins and inter- and intrahelical relationships between the proteins, thus making it difficult to design new proteins on paper. Here we present a new method of mapping out helical proteins: the Knob-Socket map. This new map lays out the entire protein helix on a 2-D map, displaying the bonding structure between the amino acids. The shading patterns displays the interaction between the separate helices. Using the Knob-Socket map, we can not only clearly map out proteins, but we can also study the effects the specific observed bonding patterns have on the proteins, where interactions might take place, as well as the folding patterns of the protein. As shown here, the α-helical coiled map shows interval clusters of knob-socket interactions, which is characteristic of the crossing-over of the helices. It is also possible to show the order in which the helices are in.