Simulation of protein crystal nucleation
โ Scribed by Matteo Pellegrini; Stephanie W. Wukovitz; Todd O. Yeates
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 132 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
โฆ Synopsis
To attempt to understand the physical principles underlying protein crystallization, an algorithm is described for simulating the crystal nucleation event computationally. The validity of the approach is supported by its ability to reproduce closely the wellknown preference of proteins for particular space group symmetries. The success of the algorithm supports a recent argument that protein crystallization is limited primarily by the entropic effects of geometric restrictions imposed during nucleation, rather than particular energetic factors. These simulations provide a new tool for attacking the problem of protein crystallization by allowing quantitative evaluation of new ideas such as the use of racemic protein mixtures.
๐ SIMILAR VOLUMES
## Abstract Simple probabilistic model for stepโwise growth of polymers is used for making some parallels with the nucleation of protein crystals. Although the considerations are made within 1D case, this approximation still shows some important peculiarities of protein crystal nucleation and growt
## Abstract Using __meanโseparationโworks__ method of Stranski and Kaischew calculations of nucleus form and energy barrier for its formation are performed for globular protein crystals. This is done on the basis of a simple model suggested for crystal nucleation of such proteins. The prerequisite
## Abstract A new method of protein nucleation and crystallization based on LangmuirโBlodgett technology is here utilized for the template stimulation of crystal growth of so far nonโcrystallized proteins. Microcrystals (60โ120 ฮผm) of bovine cytochrome P450scc and human protein kinase CKII alpha su
## Abstract With a view to experimental results on protein crystal nucleation the effects of cluster coalescence are probed semiโquantitatively. The steric association restriction, which stems from the patchy surface of the protein molecules, explains both experimentally measured low crystal nuclea