【文章內(nèi)容簡(jiǎn)介】 頻率較高，而氨基酸Ser，Qln，His頻率較低；在蛋白質(zhì)與DNA的結(jié)合位點(diǎn)中，氨基酸Arg，Trp，Gly頻率較高，氨基酸Met，Ser，F(xiàn)he，Phe，Asp頻率較低，而氨基酸His在無序區(qū)沒有出現(xiàn)；在蛋白質(zhì)與RNA的結(jié)合位點(diǎn)中氨基酸Trp，Gly頻率較高，氨基酸Met，Ser，F(xiàn)he，Pro，Asp，His頻率較低；在蛋白質(zhì)與ATP\AGP的結(jié)合位點(diǎn)中，氨基酸中Gly的頻率較高，氨基酸Al，Trp，Met，Val，Gln，Glu，Asp也有出現(xiàn)，但頻率較低，其余氨基酸沒有出現(xiàn)；在蛋白質(zhì)與輔因子的結(jié)合位點(diǎn)中，氨基酸Ala，Gln頻率較高，而氨基酸The，Phe，Asn，Pro，His，Asp沒有出現(xiàn)，其余氨基酸雖有出現(xiàn)但頻率較低；在蛋白質(zhì)與配體的結(jié)合位點(diǎn)中，氨基酸Trp，His頻率較高，而氨基酸Ala，Ser，Lys，Arg，Phe，Pro，Asp沒有出現(xiàn),其余氨基酸雖有出現(xiàn)，但頻率較低；在蛋白質(zhì)與金屬結(jié)合位點(diǎn)中，氨基酸Met，Gly，Gln，Lys出現(xiàn)的頻率較高，氨基酸Ala，Thr，Leu，Gly，Asn，Tyr，Asp出現(xiàn)的頻率較低，其余氨基酸沒有出現(xiàn)；在無序組蛋白的其它結(jié)合位點(diǎn)中，氨基酸Met，Gly，Cys出現(xiàn)頻率較高，而氨基酸Leu，Pro沒有出現(xiàn)，氨基酸Ser，Arg，Phe出現(xiàn)的頻率較低。 固有無序蛋白質(zhì)是一類具有特殊序列、結(jié)構(gòu)特征，行使特殊功能的一類特殊蛋白質(zhì)，目前成為蛋白質(zhì)研究領(lǐng)域的熱點(diǎn)之一。以上關(guān)于固有無序蛋白質(zhì)中相互作用位點(diǎn)的氨基酸偏好性分析將會(huì)為今后蛋白質(zhì)與其它分子結(jié)合位點(diǎn)預(yù)測(cè)工作提供新的思路和數(shù)據(jù)支持。隨著可得到的固有無序蛋白質(zhì)與DNA、RNA、蛋白質(zhì)復(fù)合物等結(jié)合物結(jié)構(gòu)數(shù)據(jù)的不斷增多，我們可以從原子水平上發(fā)現(xiàn)更多的相互作用過程中的規(guī)律，以加深對(duì)這種相互作用機(jī)制的理解，從而在理論上為藥物的開發(fā)和疾病的治療提供可靠的幫助。參考文獻(xiàn)[1] Uversky VN .Natively unfolded proteins: a point where biology waits for physics. Protein Sci .2002,11: 739756.[2] Dunker AK, Obradovic Z, Romero P, Garner EC, Brown CJ. Intrinsic protein disorder in plete genomes. Genome Inform Ser Workshop Genome Inform .2000, 11: 161171.[3] Dunker AK, Oldfield CJ, Meng J, Romero P, Yang JY, et al. The unfoldomics decade: an update on intrinsically disordered proteins. BMC ,9 Suppl 2: S1.[4] Nishikawa K . Natively unfolded proteins: An overview. BIOPHYSICS .2009,5: 5859.[5] Radivojac P, Iakoucheva LM, Oldfield CJ, Obradovic Z, Uversky VN, et al. Intrinsic disorder and functional proteomics. Biophys , 92: 14391456.[6] Burra PV, Kalmar L, Tompa P . Reduction in structural disorder and functional plexity in the thermal adaptation of prokaryotes. PLoS One .2010, 5: e12069.[7] PavlovicLazetic GM, Mitic NS, Kovacevic JJ, Obradovic Z, Malkov SN, et al. Bioinformatics analysis of disordered proteins in prokaryotes. BMC Bioinformatics. 2012,12: 66.[8] Xue B, Dunker AK, Uversky VN . Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life. J Biomol Struct Dyn .2012,30: 137149.[9] Sethi D, Garg A, Raghava GP. DPROT: prediction of disordered proteins using evolutionary information. Amino , 35: 599605.[10] Bellay J, Han S, Michaut M, Kim T, Costanzo M, et al. Bringing order to protein disorder through parative genomics and genetic interactions. Genome , 12: 14.[11] Muppirala UK, Honavar VG, Dobbs D Predicting RNAprotein interactions using only sequence information. BMC ,12: 489.[12] Dosztanyi Z, Csizmok V, Tompa P, Simon I The pairwise energy content estimated from amino acid position discriminates between folded and intrinsically unstructured proteins. J Mol Biol 2005,347: 827839.[13] Meszaros B, Tompa P, Simon I, Dosztanyi Z Molecular principles of the interactions of disordered proteins. J Mol Biol 2007,372: 549561.[14] Gunasekaran K, Tsai CJ, Kumar S, Zanuy D, Nussinov RExtended disordered proteins: targeting function with less scaffold. Trends Biochem Sci 2013,28: 8185.[15] 吳建盛, 棟 胡, 伍洪濤, 謝建明, 嘯 孫 蛋白質(zhì)核酸復(fù)合物界面氨基酸與核苷酸偏好性分析. 生物物理學(xué)報(bào) 2010,26: 234244.[16] Shen J, Zhang J, Luo X, Zhu W, Yu K, et proteinprotein interactions based only on sequences information. Proc Natl Acad Sci U S A 2007,104: 43374341.[17] Wu J, Liu H, Duan X, Ding Y, Wu H, et of DNAbinding residues in proteins from amino acid sequences using a random forest model with a hybrid feature. Bioinformatics 2009,25: 3035.Studies on Binding Sites Based on Sequence Characteristics Intrinsically Disordered Proteins StatisticsYan Zhiduo(College of Physics and Electronic Information, Dezhou University, Dezhou Shandong, 253023)Abstract Taking Disprot and BSDP intrinsically disordered proteins binding sites in the database as the research object, build 9 kinds of binding site data sets, using MATLAB to statistics the binding sites of various amino acids frequency, it was found that the interaction sites of protein and protein is the most, interaction sites of proteins and ATP/GTP is the least, and we can learn that all kinds of binding site of amino acid has obvious preferences. The study is helpful to know the intrinsically chaotic characteristics of protein interactions wi