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Karen R. Khar

Researcher at University of Kansas

Publications -  5
Citations -  540

Karen R. Khar is an academic researcher from University of Kansas. The author has contributed to research in topics: Denaturation (biochemistry) & Protein folding. The author has an hindex of 4, co-authored 5 publications receiving 220 citations. Previous affiliations of Karen R. Khar include Fox Chase Cancer Center.

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Journal ArticleDOI

Macromolecular modeling and design in Rosetta: recent methods and frameworks

Julia Koehler Leman, +117 more
- 01 Jul 2020 - 
TL;DR: This Perspective reviews tools developed over the past five years in the Rosetta software, including over 80 methods, and discusses improvements to the score function, user interfaces and usability.
Journal ArticleDOI

Fully Flexible Docking of Medium Sized Ligand Libraries with RosettaLigand

TL;DR: Improved initial placement of the ligand is critical for successful prediction of an accurate binding position in the ‘high-resolution’ full atom refinement step, making RosettaLigand appropriate for docking medium sized ligand libraries.
Journal ArticleDOI

Fast Docking on Graphics Processing Units via Ray-Casting

TL;DR: In this article, the authors describe an adaptation of DARC for use on Graphics Processing Units (GPUs), leading to a speedup of approximately 27-fold in typical use cases over the corresponding calculations carried out using a CPU alone.
Journal ArticleDOI

Chaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone Proteins.

TL;DR: A rapid method for assessing the kinetic stability of folded proteins and monitoring the effects of ligand stabilization for both intrinsically stable proteins and metastable proteins that uses a new GroEL chaperonin-based biolayer interferometry (BLI) denaturant pulse platform is described.
Book ChapterDOI

Constructing Kinetically Controlled Denaturation Isotherms of Folded Proteins Using Denaturant-Pulse Chaperonin Binding.

TL;DR: A label-free method is described that examines the denaturation of immobilized proteins where the dynamic unfolded protein populations are captured and detected by chaperonin binding.