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
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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