Proteins that consist of multiple domains, or units with discrete biological functions, are prevalent in nature. These domains are connected by linker regions whose sequences and lengths have evolved to position them appropriately for their functions. However, these linker regions may be flexible and challenging to characterize, and the advantages that particular linker lengths and compositions provide remain poorly understood. I study the importance of linker regions in the model protein MoCVNH-LysM using a combination of Nuclear Magnetic Resonance spectroscopy and Molecular Dynamics simulation.
University of Pittsburgh, Bachelor of Science in Chemistry and Molecular Biology, 2009
Carnegie Mellon University, MChE in Chemical Engineering, 2010
PhD Advisors: Dr. Angela Gronenborn & Dr. Lillian Chong
- Jun S, Ke D, Debiec K, Zhao G, Meng X, Ambrose Z, Gibson GA, Watkins SC, Zhang P. Direct visualization of HIV-1 with correlative live-cell microscopy and cryo-electron tomography. Structure. 2011; 19(11):1573-81.
- Debiec KT, Gronenborn AM, Chong LT. Evaluating the strength of salt bridges: a comparison of current biomolecular force fields. J Phys Chem B. 2014;118(24):6561-9
- Korotchenko VN, Saydmohammed M, Vollmer LL, Bakan A, Sheetz K, Debiec KT, Greene KA, Agliori CS, Bahar I, Day BW, Vogt A, Tsang M. (2014) In vivo structure-activity relationship studies support allosteric targeting of a dual specificity phosphatase. Chembiochem 2014; 15(10):1436-45
- Koharudin LM, Debiec KT, Gronenborn AM. (2015) Structural Insight into Fungal Cell Wall Recognition by a CVNH Protein with a Single LysM Domain. Structure, 23(11):2143-54
- Debiec KT, Cerutti DS, Baker LR, Gronenborn AM, Case DA, Chong LT. (2016) Further along the Road Less Traveled: AMBER ff15ipq, an Original Protein Force Field Built on a Self-Consistent Physical Model. J Chem Theory Comput. 12(8):3926-47