profile photo of Kenneth McGuinness in front of tree

Kenneth N. McGuinness, PhD

Postdoctoral Associate

Education

BA Biomathematics, Rutgers University, 2010
PhD Computational Biology and Molecular Biophysics, Rutgers University, 2016

Bio

Kenneth has a PhD in Computational Biology and Molecular Biophysics from Rutgers University. During his PhD studies at CABM, he focused on how hydrophobicity can be tuned to modulate collagen-like peptide supramolecular assembly. After his PhD studies, Kenneth was awarded a Merck Inc., & Co. Postdoctoral Fellowship. At Merck, Kenneth applied machine learning to the study of predicting changes in protein thermostability due to single amino acid substitutions. Realizing his dream of teaching and performing science with undergraduates, he went back to academia, was awarded an NIH IRACDA fellowship, and was recently hired as an Assistant Professor of Biology at Caldwell University in Caldwell NJ, starting in fall 2022. As an IRACDA fellow, Kenneth worked at CABM in Dr. Vikas Nanda’s lab studying the structural evolution of metal sites within proteins and minerals.

Research Focus

Metalloproteins and the coevolution of the biosphere and geosphere. Scientific teaching strategies

NIH IRACDA Postdoctoral Fellow

Merck Inc., & Co. Postdoctoral Fellow

Gunnar W. Klau, Heinrich-Heine-Universität Düsseldorf

Eli K. Moore, Rowan University

Shaunna Morrison, Carnegie Institute for Science

McGuinness K, Pan W, Sheridan R, Murphy G, Crespo A. Role of simple descriptors and applicability domain in predicting change in protein thermostability. PloS one. 2018;13(9):e0203819. doi:10.1371/journal.pone.0203819.
McGuinness K, Nanda V. Collagen mimetic peptide discs promote assembly of a broad range of natural protein fibers through hydrophobic interactions. Organic & biomolecular chemistry. 2017;15(28):5893-5898. doi:10.1039/c7ob01073g.
McGuinness K. Morphological diversity and polymorphism of self-assembling collagen peptides controlled by length of hydrophobic domains. ACS nano. 2014;8(12):12514-23. doi:10.1021/nn505369d.