Knob-Socket Mapping of a-Helical Proteins
Poster Number
29
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
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.