分子生物物理學(xué)(完整版)
【正文】 e protein3. Antibody recognition, phosphorylation, glycosylation, hydroxylation Gammaturn1. Hbond: ii+22. (70, 60) and (70, 60) for i+1 residueTypeII’secondary3JHAHN righthanded ahelix, phi = 57, 3JHAHN = Hz right handed helix, phi = 60, 3JHAHN = Hz antiparallel ?sheet, phi = 139, 3JHAHN = Hz parallel ?sheet, phi = 119, 3JHAHN = Hz lefthanded ahelix, phi = 57, 3JHAHN = HzPrediction結(jié)構(gòu)層次。 ? （ 2）對(duì)于較大的球狀蛋白質(zhì)或亞基，其三級(jí)結(jié)構(gòu)往往由兩個(gè)或多個(gè)結(jié)構(gòu)域締合而成也即它們是多結(jié)構(gòu)域的，例如免疫球蛋白的輕鏈含 2個(gè)結(jié)構(gòu)域。嗜熱菌蛋白酶與人碳酸酐酶的結(jié)構(gòu)圖嗜熱菌蛋白酶與人碳酸酐酶的結(jié)構(gòu)圖研究蛋白質(zhì)三級(jí)結(jié)構(gòu)的方法研究蛋白質(zhì)三級(jí)結(jié)構(gòu)的方法 X射線晶體衍射（ Xray crystallography) 多維核磁共振 ( multidimensional NMR) 三維電子顯微鏡技術(shù)（ 3dimensiional EM) 掃描探針顯微術(shù) ( Scanning Probe Microscopy ,SPM) ProteinStructure 獨(dú)立的三級(jí)結(jié)構(gòu)之間的非共價(jià)締合稱為四級(jí)結(jié)構(gòu)。功能域可以是一個(gè)結(jié)構(gòu)域，也可以是由兩個(gè)結(jié)構(gòu)域或兩個(gè)以上結(jié)構(gòu)域組成，從功能角度看許多多結(jié)構(gòu)域的酶，其活性中心都位于結(jié)構(gòu)域之間，因?yàn)橥ㄟ^結(jié)構(gòu)域容易構(gòu)建具有特定三維排布的活性中心。 。secondarywithout) helix, respectively. The backbone dihedral angles of residue are (60, 30) and (60, 30) of residues i+1 and i+2, respectively of the classical type III turn. .andofdesign projects by Degrado, USAHelicalstructure?helicesinandhydrogennearlythestandardareprotein?the dipoles of hydrogen bonding backbone atoms are in near perfect alignment. the radius ( angstrom)of the helix allows for favorable van der Waals interactions across the helical axis side chains are well staggered minimizing steric interference? CO group toward carboxyl terminus? NH group toward amide terminus? Hbond, i(i+4)? Side chain: i(i+3)。, . the ahelix has a rise per residue of 197。41structure[n] is the number of residues per helical turn[r] is the helical rise per residue (nm)[p] is the helical pitch (nm). Hbond Atoms in Hbond loopradius i, i+4 13 310 i, i+3 10 ? i, i+5 16 Parametersnm Hbond definition, Hbond location O….H XHydrogen6Relation wit
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