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Protein folding and de novo protein design for biotechnological applications

Author(s): Khoury, George A; Smadbeck, James; Kieslich, Chris A; Floudas, Christodoulos A

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dc.contributor.authorKhoury, George A-
dc.contributor.authorSmadbeck, James-
dc.contributor.authorKieslich, Chris A-
dc.contributor.authorFloudas, Christodoulos A-
dc.date.accessioned2021-10-08T19:58:55Z-
dc.date.available2021-10-08T19:58:55Z-
dc.date.issued2014-02en_US
dc.identifier.citationKhoury, George A., James Smadbeck, Chris A. Kieslich, and Christodoulos A. Floudas. "Protein folding and de novo protein design for biotechnological applications." Trends in Biotechnology 32, no. 2 (2014): 99-109. doi:10.1016/j.tibtech.2013.10.008en_US
dc.identifier.issn0167-7799-
dc.identifier.urihttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3922204/-
dc.identifier.urihttp://arks.princeton.edu/ark:/88435/pr1z56r-
dc.description.abstractIn the postgenomic era, the medical/biological fields are advancing faster than ever. However, before the power of full-genome sequencing can be fully realized, the connection between amino acid sequence and protein structure, known as the protein folding problem, needs to be elucidated. The protein folding problem remains elusive, with significant difficulties still arising when modeling amino acid sequences lacking an identifiable template. Understanding protein folding will allow for unforeseen advances in protein design; often referred to as the inverse protein folding problem. Despite challenges in protein folding, de novo protein design has recently demonstrated significant success via computational techniques. We review advances and challenges in protein structure prediction and de novo protein design, and highlight their interplay in successful biotechnological applications.en_US
dc.format.extent99 - 109en_US
dc.language.isoen_USen_US
dc.relation.ispartofTrends in Biotechnologyen_US
dc.rightsAuthor's manuscripten_US
dc.titleProtein folding and de novo protein design for biotechnological applicationsen_US
dc.typeJournal Articleen_US
dc.identifier.doidoi:10.1016/j.tibtech.2013.10.008-
dc.identifier.eissn1879-3096-
pu.type.symplectichttp://www.symplectic.co.uk/publications/atom-terms/1.0/journal-articleen_US

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