Helix-Helix Loop Closure Quailty

Florian Wieser*, Gustav Oberdorfer

*Corresponding author for this work

Research output: Contribution to conferencePosterpeer-review

Abstract

The helix bundle is a structural protein motif commonly found in nature in a variety of functional roles ranging from cytochromes to DNA-binding proteins. Due to its functional flexibility, its structural stability as well as its well defined secondary structure, the helix bundle is a promising candidate to be deployed as a scaffold for functional protein designs.
Helix bundles are composed of usually two to several parallel or antiparallel alpha helices connected by structurally poor defined loop regions. If not designed carefully, these loop regions can be potential source of decreased protein stability and subsequently impaired folding capability. Judging the quality of all loops present in a set of helix bundle designs manually emerges as cumbersome, not at least because of the unstructured nature of loops. Here I present my early work on a simple metric for RosettaScripts that should capture quality features of loops within helix bundles.
Translated title of the contributionQualitaet von Helix-Helix Loop-Verbindungen
Original languageEnglish
Number of pages1
Publication statusPublished - 15 Mar 2021
EventWinterRosettaCon 2021 - Virtuell, United States
Duration: 15 Mar 202118 Mar 2021

Conference

ConferenceWinterRosettaCon 2021
Country/TerritoryUnited States
CityVirtuell
Period15/03/2118/03/21

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