Computational approaches to study protein unfolding: Hen egg white lysozyme as a case study

Proteins: Structure, Function and Bioinformatics - Tập 21 Số 3 - Trang 196-213 - 1995
Philippe H. Hünenberger1, Alan E. Mark1, Wilfred F. van Gunsteren1
1Laboratorium für Physikalische Chemie, ETH- Zentrum, CH-8092 Zürich, Switzerland

Tóm tắt

AbstractFour methods are compared to drive the unfolding of a protein: (1) high temperature (T‐run), (2) high pressure (P‐run), (3) by imposing a gradual increase in the mean radius of the protein using a penalty function added to the physical interaction function (F‐run, radial force driven unfolding), and (4) by weak coupling of the difference between the temperature of the radially outward moving atoms and the radially inward moving atoms to an external temperature bath (K‐run, kinetic energy driven unfolding). The characteristic features of the four unfolding pathways are analyzed in order to detect distortions due to the size or the type of the applied perturbation, as well as the features that are common to all of them. Hen egg white lysozyme is used as a test system. The simulations are analyzed and compared to experimental data like 1H‐NMR amide proton exchange‐folding competition, heat capacity, and compressibility measurements. © 1995 Wiley‐Liss, Inc.

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Proteins: Structure, Function and Bioinformatics

Tập 21 Số 3

196-213

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