the number of peaks), together with their amplitudes (from the peak areas), time constant values (from the We show that numerical inversion of the Laplace transform by using the maximum entropy method can peak positions), and associated Monte Carlo uncertainties. On the other hand, recent theoretica
Equilibrium protein folding-unfolding process involving multiple intermediates
✍ Scribed by Hui-Chih Hung; Yu-Hou Chen; Guang-Yaw Liu; Hwei-Jen Lee; Gu-Gang Chang
- Publisher
- Springer
- Year
- 2003
- Tongue
- English
- Weight
- 302 KB
- Volume
- 65
- Category
- Article
- ISSN
- 1522-9602
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✦ Synopsis
Mathematical models for the protein folding-unfolding process involving multiple intermediates have been derived. Computer fitting of the experimental data to this model generates various thermodynamic parameters for the folding-unfolding process. In this way, the complex folding-unfolding process of the multi-domain proteins can be analysed in a quantitative way. The application of the folding-unfolding model involving seven stages in human placental alkaline phosphatase is described.
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The equilibrium of protein folding-unfolding has been investigated with a simple two-state, native and random-coil, model; we have termed this the globule-coil model. Energies are calculated by favoring native long-range contact pairs. Most-probable native domains are obtained a t all stages of the
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
## Abstract The molten globule model for the beginning of the folding process, which originated with Kuwajima's studies of __α__‐lactalbumin (Kuwajima, K., 1989, __Proteins Struct. Funct. Genet. 6__, 87–103, and references therein), states that, for those proteins that exhibit equilibrium molten gl
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