How fast-folding proteins fold

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How fast-folding proteins fold. / Lindorff-Larsen, Kresten; Piana, Stefano; Dror, Ron O; Shaw, David E.

In: Science (New York, N.Y.), Vol. 334, No. 6055, 2011, p. 517-20.

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

Harvard

Lindorff-Larsen, K, Piana, S, Dror, RO & Shaw, DE 2011, 'How fast-folding proteins fold', Science (New York, N.Y.), vol. 334, no. 6055, pp. 517-20. https://doi.org/10.1126/science.1208351

APA

Lindorff-Larsen, K., Piana, S., Dror, R. O., & Shaw, D. E. (2011). How fast-folding proteins fold. Science (New York, N.Y.), 334(6055), 517-20. https://doi.org/10.1126/science.1208351

Vancouver

Lindorff-Larsen K, Piana S, Dror RO, Shaw DE. How fast-folding proteins fold. Science (New York, N.Y.). 2011;334(6055):517-20. https://doi.org/10.1126/science.1208351

Author

Lindorff-Larsen, Kresten ; Piana, Stefano ; Dror, Ron O ; Shaw, David E. / How fast-folding proteins fold. In: Science (New York, N.Y.). 2011 ; Vol. 334, No. 6055. pp. 517-20.

Bibtex

@article{1df1faacde454a61979b7378d5d1d44d,
title = "How fast-folding proteins fold",
abstract = "An outstanding challenge in the field of molecular biology has been to understand the process by which proteins fold into their characteristic three-dimensional structures. Here, we report the results of atomic-level molecular dynamics simulations, over periods ranging between 100 µs and 1 ms, that reveal a set of common principles underlying the folding of 12 structurally diverse proteins. In simulations conducted with a single physics-based energy function, the proteins, representing all three major structural classes, spontaneously and repeatedly fold to their experimentally determined native structures. Early in the folding process, the protein backbone adopts a nativelike topology while certain secondary structure elements and a small number of nonlocal contacts form. In most cases, folding follows a single dominant route in which elements of the native structure appear in an order highly correlated with their propensity to form in the unfolded state.",
author = "Kresten Lindorff-Larsen and Stefano Piana and Dror, {Ron O} and Shaw, {David E}",
year = "2011",
doi = "10.1126/science.1208351",
language = "English",
volume = "334",
pages = "517--20",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6055",

}

RIS

TY - JOUR

T1 - How fast-folding proteins fold

AU - Lindorff-Larsen, Kresten

AU - Piana, Stefano

AU - Dror, Ron O

AU - Shaw, David E

PY - 2011

Y1 - 2011

N2 - An outstanding challenge in the field of molecular biology has been to understand the process by which proteins fold into their characteristic three-dimensional structures. Here, we report the results of atomic-level molecular dynamics simulations, over periods ranging between 100 µs and 1 ms, that reveal a set of common principles underlying the folding of 12 structurally diverse proteins. In simulations conducted with a single physics-based energy function, the proteins, representing all three major structural classes, spontaneously and repeatedly fold to their experimentally determined native structures. Early in the folding process, the protein backbone adopts a nativelike topology while certain secondary structure elements and a small number of nonlocal contacts form. In most cases, folding follows a single dominant route in which elements of the native structure appear in an order highly correlated with their propensity to form in the unfolded state.

AB - An outstanding challenge in the field of molecular biology has been to understand the process by which proteins fold into their characteristic three-dimensional structures. Here, we report the results of atomic-level molecular dynamics simulations, over periods ranging between 100 µs and 1 ms, that reveal a set of common principles underlying the folding of 12 structurally diverse proteins. In simulations conducted with a single physics-based energy function, the proteins, representing all three major structural classes, spontaneously and repeatedly fold to their experimentally determined native structures. Early in the folding process, the protein backbone adopts a nativelike topology while certain secondary structure elements and a small number of nonlocal contacts form. In most cases, folding follows a single dominant route in which elements of the native structure appear in an order highly correlated with their propensity to form in the unfolded state.

U2 - 10.1126/science.1208351

DO - 10.1126/science.1208351

M3 - Journal article

C2 - 22034434

VL - 334

SP - 517

EP - 520

JO - Science

JF - Science

SN - 0036-8075

IS - 6055

ER -

ID: 37812270