Experimental Parameterization of an Energy Function for the Simulation of Unfolded Proteins
β Scribed by Norgaard, Anders B.; Ferkinghoff-Borg, Jesper; Lindorff-Larsen, Kresten
- Book ID
- 119921193
- Publisher
- Biophysical Society
- Year
- 2008
- Tongue
- English
- Weight
- 336 KB
- Volume
- 94
- Category
- Article
- ISSN
- 0006-3495
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π SIMILAR VOLUMES
We analyzed several energy functions for predicting the native state of proteins from an energy minimization procedure. We derived the parameters of a given energy function by imposing the basic requirement that the energy of the native conformation of a protein is lower than that of any conformatio
We have calculated the free energy of a spherical model of a protein or part of a protein generated in the way of protein folding. Two spherical models are examined; one is a homogeneous model consisting of only one residue type-hydrophobic. The other is a heterogeneous model consisting of two resid
It is quite easy to propose an empirical potential for conformational analysis such that given crystal structures lie near local minima. What is much more difficult, is to devise a function such that the native structure lies near a relatively deep local minimum, at least in some neighborhood of the