IMR Press / FBL / Volume 9 / Issue 5 / DOI: 10.2741/1435

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Computational protein chemistry of p53 and p53 peptides
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1 Department of Environmental Health Sciences, Mailman School of Public Health, Columbia University, New York, NY 10032
2 Experimental Therapeutics Program, Division of Medical Oncology, College of Physicians and Surgeons, Columbia University, New York, NY 10032
3 Department of Pathology and Laboratory Medicine, Harbor VA Medical Center and Department of Pathology, SUNY Downstate Medical Center, New York, NY 11203
Academic Editor:Mathew Pincus
Front. Biosci. (Landmark Ed) 2004, 9(5), 2778–2787;
Published: 1 September 2004

Computational protein chemistry has potential to contribute to the development of new therapeutic approaches in medicine in several different ways, including indirectly by increasing understanding of the disease-associated changes in protein structure that are mechanistically important, which can have diagnostic implications, as well as directly in designing peptides to counteract the patho-physiologic effects of these changes. Studies of the role of the tumor suppressor protein p53 in the carcinogenic process provide examples of both types of contribution. Computational studies of the effects of mutations in p53 on its structure have provided insights into cancer mechanisms and have served to elucidate potential new diagnostic approaches based on the identification of changes in p53 structure. Computational studies of p53 peptides have contributed to identifying and optimizing the structural characteristics that contribute to their activity in selectively killing cancer cells.

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