High thermodynamic stability of parametrically designed helical bundles

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

High thermodynamic stability of parametrically designed helical bundles. / Huang, Po Ssu; Oberdorfer, Gustav; Xu, Chunfu; Pei, Xue Y.; Nannenga, Brent L.; Rogers, Joseph M.; DiMaio, Frank; Gonen, Tamir; Luisi, Ben; Baker, David.

In: Science, Vol. 346, No. 6208, 24.10.2014, p. 481-485.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Huang, PS, Oberdorfer, G, Xu, C, Pei, XY, Nannenga, BL, Rogers, JM, DiMaio, F, Gonen, T, Luisi, B & Baker, D 2014, 'High thermodynamic stability of parametrically designed helical bundles', Science, vol. 346, no. 6208, pp. 481-485. https://doi.org/10.1126/science.1257481

APA

Huang, P. S., Oberdorfer, G., Xu, C., Pei, X. Y., Nannenga, B. L., Rogers, J. M., DiMaio, F., Gonen, T., Luisi, B., & Baker, D. (2014). High thermodynamic stability of parametrically designed helical bundles. Science, 346(6208), 481-485. https://doi.org/10.1126/science.1257481

Vancouver

Huang PS, Oberdorfer G, Xu C, Pei XY, Nannenga BL, Rogers JM et al. High thermodynamic stability of parametrically designed helical bundles. Science. 2014 Oct 24;346(6208):481-485. https://doi.org/10.1126/science.1257481

Author

Huang, Po Ssu ; Oberdorfer, Gustav ; Xu, Chunfu ; Pei, Xue Y. ; Nannenga, Brent L. ; Rogers, Joseph M. ; DiMaio, Frank ; Gonen, Tamir ; Luisi, Ben ; Baker, David. / High thermodynamic stability of parametrically designed helical bundles. In: Science. 2014 ; Vol. 346, No. 6208. pp. 481-485.

Bibtex

@article{6a8253ff269348248e51ecd9f253e600,
title = "High thermodynamic stability of parametrically designed helical bundles",
abstract = "We describe a procedure for designing proteins with backbones produced by varying the parameters in the Crick coiled coil-generating equations. Combinatorial design calculations identify low-energy sequences for alternative helix supercoil arrangements, and the helices in the lowest-energy arrangements are connected by loop building. We design an antiparallel monomeric untwisted three-helix bundle with 80-residue helices, an antiparallel monomeric right-handed four-helix bundle, and a pentameric parallel left-handed five-helix bundle. The designed proteins are extremely stable (extrapolated ΔGfold > 60 kilocalories per mole), and their crystal structures are close to those of the design models with nearly identical core packing between the helices. The approach enables the custom design of hyperstable proteins with fine-tuned geometries for a wide range of applications.",
author = "Huang, {Po Ssu} and Gustav Oberdorfer and Chunfu Xu and Pei, {Xue Y.} and Nannenga, {Brent L.} and Rogers, {Joseph M.} and Frank DiMaio and Tamir Gonen and Ben Luisi and David Baker",
year = "2014",
month = oct,
day = "24",
doi = "10.1126/science.1257481",
language = "English",
volume = "346",
pages = "481--485",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6208",

}

RIS

TY - JOUR

T1 - High thermodynamic stability of parametrically designed helical bundles

AU - Huang, Po Ssu

AU - Oberdorfer, Gustav

AU - Xu, Chunfu

AU - Pei, Xue Y.

AU - Nannenga, Brent L.

AU - Rogers, Joseph M.

AU - DiMaio, Frank

AU - Gonen, Tamir

AU - Luisi, Ben

AU - Baker, David

PY - 2014/10/24

Y1 - 2014/10/24

N2 - We describe a procedure for designing proteins with backbones produced by varying the parameters in the Crick coiled coil-generating equations. Combinatorial design calculations identify low-energy sequences for alternative helix supercoil arrangements, and the helices in the lowest-energy arrangements are connected by loop building. We design an antiparallel monomeric untwisted three-helix bundle with 80-residue helices, an antiparallel monomeric right-handed four-helix bundle, and a pentameric parallel left-handed five-helix bundle. The designed proteins are extremely stable (extrapolated ΔGfold > 60 kilocalories per mole), and their crystal structures are close to those of the design models with nearly identical core packing between the helices. The approach enables the custom design of hyperstable proteins with fine-tuned geometries for a wide range of applications.

AB - We describe a procedure for designing proteins with backbones produced by varying the parameters in the Crick coiled coil-generating equations. Combinatorial design calculations identify low-energy sequences for alternative helix supercoil arrangements, and the helices in the lowest-energy arrangements are connected by loop building. We design an antiparallel monomeric untwisted three-helix bundle with 80-residue helices, an antiparallel monomeric right-handed four-helix bundle, and a pentameric parallel left-handed five-helix bundle. The designed proteins are extremely stable (extrapolated ΔGfold > 60 kilocalories per mole), and their crystal structures are close to those of the design models with nearly identical core packing between the helices. The approach enables the custom design of hyperstable proteins with fine-tuned geometries for a wide range of applications.

UR - http://www.scopus.com/inward/record.url?scp=84908235298&partnerID=8YFLogxK

U2 - 10.1126/science.1257481

DO - 10.1126/science.1257481

M3 - Journal article

C2 - 25342806

AN - SCOPUS:84908235298

VL - 346

SP - 481

EP - 485

JO - Science

JF - Science

SN - 0036-8075

IS - 6208

ER -

ID: 244651037