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Designing new protein structures and functions with the molecular modeling program Rosetta
Author(s) -
Kuhlman Brian
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.350.1
Subject(s) - protein design , protein engineering , computational biology , computer science , function (biology) , protein structure , set (abstract data type) , structural bioinformatics , biology , biochemistry , microbiology and biotechnology , programming language , enzyme
Proteins perform an amazingly diverse set of functions in all aspects of life. Critical to the function of many proteins are the highly specific three‐dimensional structures they adopt. For this reason, there is strong interest in learning how to rationally design proteins that adopt user‐defined structures. Over the last 20‐years there has been significant progress by us and others in the field of computational protein design as rotamer‐based sequence optimization protocols have been used to accurately design protein tertiary and quaternary structure. I will summarize how the molecular modeling program Rosetta is used to design new protein structures and describe how we have used this capability to create proteins that have important applications in research and medicine. I will highlight three protein design stories: (1) the engineering of light‐inducible proteins that can be used to recruit proteins to specific locations in the cell, (2) the use of protein interface design to create therapeutic bispecific antibodies, and (3) the de novo design of new protein structures from pieces of naturally occurring proteins. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .