Covalent Modification as Targets and Means for Research in Intrinsically Disordered Proteins
Research Mentor(s)
Dr. Serge Smirnov
Description
A reported 33% of eukaryotic proteins are predicted to contain intrinsically disordered regions (IDRs) over 30 residues in length. IDRs are regions of protein which natively exist in an unfolded conformation. Due to their highly dynamic nature, many common methods of inquiry such as crystallography and NMR can be thwarted. As a result, valuable analysis such as probing function, dynamics and binding interfaces are unable to be performed. To minimize these problems, researchers typically study shorter IDRs. We probed fragments of plant protein villin isoform 4 for covalent modifications to explore its regulation and degradation. Disordered regions of proteins have greater solvent accessibility compared to their folded counterparts. This results in various post translational modifications, a common method of protein regulation. The protein villin isoform 4 (VLN4) is vital to the development of roots and understanding its regulation could greatly benefit agriculture. Thus, VLN4 was examined for degradation, ubiquitination, and phosphorylation.
Document Type
Event
Start Date
May 2022
End Date
May 2022
Location
Carver Gym (Bellingham, Wash.)
Department
CSE - Chemistry
Genre/Form
student projects; posters
Type
Image
Rights
Copying of this document in whole or in part is allowable only for scholarly purposes. It is understood, however, that any copying or publication of this document for commercial purposes, or for financial gain, shall not be allowed without the author’s written permission.
Language
English
Format
application/pdf
Covalent Modification as Targets and Means for Research in Intrinsically Disordered Proteins
Carver Gym (Bellingham, Wash.)
A reported 33% of eukaryotic proteins are predicted to contain intrinsically disordered regions (IDRs) over 30 residues in length. IDRs are regions of protein which natively exist in an unfolded conformation. Due to their highly dynamic nature, many common methods of inquiry such as crystallography and NMR can be thwarted. As a result, valuable analysis such as probing function, dynamics and binding interfaces are unable to be performed. To minimize these problems, researchers typically study shorter IDRs. We probed fragments of plant protein villin isoform 4 for covalent modifications to explore its regulation and degradation. Disordered regions of proteins have greater solvent accessibility compared to their folded counterparts. This results in various post translational modifications, a common method of protein regulation. The protein villin isoform 4 (VLN4) is vital to the development of roots and understanding its regulation could greatly benefit agriculture. Thus, VLN4 was examined for degradation, ubiquitination, and phosphorylation.