Specific and non-specific contacts in protein crystals.
Statistical analysis of protein-protein interfaces in a database of pure peptide crystals shows that the distribution of the contact area contains two components: a major exponential distribution and a minor flat distribution. Analysis of two sub-databases provides evidence that the two components represent specific and non-specific contacts, respectively. The probability of an interface with a given area being specific can be estimated. A scaled quantity (contact ratio) is introduced that is more useful than contact area for discriminating specific and non-specific contacts in protein crystals.
Dan
Feng
F
Center of Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China. fengdan_bj@yahoo.com
Zong-Hao
Zeng
Z
D001665:Binding Sites; D019295:Computational Biology; D003460:Crystallization; D018360:Crystallography, X-Ray; D030562:Databases, Protein; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity
D011506:Proteins