Bioinformatics study on protein structures – UROP Spring Symposium 2021

Bioinformatics study on protein structures

Ava Pardo-Keegan


Pronouns: She/Her/Hers

Research Mentor(s): Yang Zhang, Professor
Research Mentor School/College/Department: Department of Computational Medicine & Bioinformatics, Michigan Medicine
Presentation Date: Thursday, April 22, 2021
Session: Session 1 (10am-10:50am)
Breakout Room: Room 17
Presenter: 3

Event Link


The majority of proteins are composed of foldable, stable subunits called domains. The structures of these proteins can be made up of a single domain or multiple domains. Determining structures of multidomain proteins is a crucial step in elucidating their functions and designing new drugs to regulate these functions. However, it has been largely ignored by the mainstream of computational biology due to the difficulty in modeling inter-domain interactions. Therefore, almost all of the advanced protein structure prediction methods are optimized for modeling single domain proteins. In this study, we presented a method to construct a multidomain protein structure library with known full-length structures to assist the multidomain protein structure prediction. We collect all multidomain proteins from the Protein Data Bank based on the DomainParser, and multidomain proteins defined in CATH and SCOPe databases are also included in the library. This resulted in a total of 15,293 multidomain proteins in the library. The completeness of the library is examined by structurally matching a set of non-redundant multidomain proteins through the library using TM-align. The results show that most of the cases can obtain at least 1 template with correct global fold (TM-score >0.5) from the library, which indicates that the constructed multidomain protein library can likely be used to guide the multidomain protein structure modeling.

Authors: Ava Pardo-Keegan, Xiaogen Zhou, Yang Zhang
Research Method: Computer Programming

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