Structure of the calcium regulatory muscle protein troponin-C at 2.8 A resolution

Crystals of turkey skeletal muscle troponin-C reveal a molecule of two domains with an unusual structure. Two Ca2+ ions are bound to the C-terminal domain. The two cation-binding sites of the regulatory (N-terminal) domain are Ca2+ free; this domain adopts a markedly different conformation from the C-terminal domain. The two domains are connected by a long nine-turn alpha-helix; three of these turns are exposed fully to solvent.     

Three-dimensional structure of an antigen-antibody complex at 6 A resolution

Present understanding of the three-dimensional structure of antibody combining sites is based on X-ray diffraction studies of myeloma immunoglobulins. The structures of the antigen-binding fragment (Fab) complexes of two of these immunoglobulins with small ligands have also been determined. However, there is no crystallographic information concerning the interactions of an antibody with an antigen, nor do we know the precise structure of antigenic determinants on protein molecules. We now report the first structure determination of an antigen-antibody complex at 6 A resolution. The structure of the complex between hen egg-white lysozyme and the Fab of a monoclonal anti-lysozyme antibody (D1.3) shows that the combining site of antibodies is not merely a cleft delineated by the complementarity-determining regions of the variable regions of the light and heavy chains, but is a larger area extending beyond it. A correspondingly large area of the antigen makes close contacts with the antibody, in agreement with the notion of a 'topographical' rather than 'sequential' antigenic determinant. The structural basis of cross-reactivities of an antibody with heterologous antigens and the effect of a single amino acid substitution on antigenic specificity can thus be visualized in the structural model presented here.     

Three-dimensional structure of cyanobacterial photosystem I at 2.5 A resolution.

Life on Earth depends on photosynthesis, the conversion of light energy from the Sun to chemical energy. In plants, green algae and cyanobacteria, this process is driven by the cooperation of two large protein-cofactor complexes, photosystems I and II, which are located in the thylakoid photosynthetic membranes. The crystal structure of photosystem I from the thermophilic cyanobacterium Synechococcus elongatus described here provides a picture at atomic detail of 12 protein subunits and 127 cofactors comprising 96 chlorophylls, 2 phylloquinones, 3 Fe4S4 clusters, 22 carotenoids, 4 lipids, a putative Ca2+ ion and 201 water molecules. The structural information on the proteins and cofactors and their interactions provides a basis for understanding how the high efficiency of photosystem I in light capturing and electron transfer is achieved.     

Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands.

The crystal structure of the met repressor-operator complex shows two dimeric repressor molecules bound to adjacent sites 8 base pairs apart on an 18-base-pair DNA fragment. Sequence specificity is achieved by insertion of double-stranded antiparallel protein beta-ribbons into the major groove of B-form DNA, with direct hydrogen-bonding between amino-acid side chains and the base pairs. The repressor also recognizes sequence-dependent distortion or flexibility of the operator phosphate backbone, conferring specificity even for inaccessible base pairs.     

Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2.

The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides the first complete view of the extracellular region of a cell adhesion molecule. The topology of the molecule, which comprises two immunoglobulin-like domains, is the same as that of the first two domains of CD4 but the relative domain orientation is altered by a fairly flexible linker region. The putative ligand-binding beta-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction.     

(±)-1,2-二苯基乙二胺的合成与拆分

探讨 (± ) -1 ,2 -二苯基乙二胺 (3 )的几种合成路径 ,选择路线四来合成化合物 (3 ) ,并经 (-) -酒石酸拆分得到了 ( ) -1 ,2 -二苯基乙二胺 ,该路线具有原料易得、反应易控制、收率高、生产操作安全性好等特点 ,所得化合物经 MS、IR、1 HNMR等表征 ,结构正确 ,产品纯度经气相色谱分析达到 99.0 %以上 .     

X-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes

Knowledge of the tertiary structure of the proteinase from human immunodeficiency virus HIV-1 is important to the design of inhibitors that might possess antiviral activity and thus be useful in the treatment of AIDS. The conserved Asp-Thr/Ser-Gly sequence in retroviral proteinases suggests that they exist as dimers similar to the ancestor proposed for the pepsins. Although this has been confirmed by X-ray analyses of Rous sarcoma virus and HIV-1 proteinases, these structures have overall folds that are similar to each other only where they are also similar to the pepsins. We now report a further X-ray analysis of a recombinant HIV-1 proteinase at 2.7 A resolution. The polypeptide chain adopts a fold in which the N- and C-terminal strands are organized together in a four-stranded beta-sheet. A helix precedes the single C-terminal strand, as in the Rous sarcoma virus proteinase and also in a synthetic HIV-1 proteinase, in which the cysteines have been replaced by alpha-aminobuytric acid. The structure reported here provides an explanation for the amino acid invariance amongst retroviral proteinases, but differs from that reported earlier in some residues that are candidates for substrate interactions at P3, and in the mode of intramolecular cleavage during processing of the polyprotein.     

径向l-1乘子有界性的L~1标准

讨论了径向l-1乘子有界性的L1 标准 .给出了函数为径向l-1 乘子的充分条件     

傅立叶变换光谱仪理论分辨率的一种新诠释

从光学变迹函数的角度对傅立叶变换光谱仪（Ｆｏｕｉｅｒ Ｔｒａｎｓｆｏｒｍ Ｓｐｅｃｔｒｏｍｅｔｅｒ,简称ＦＴＳ）Ｒ 理论分辨极限进行了新的推导和诠释,揭示了光学变迹函数与ＦＴＳ的仪器函数之间的内在联系,对深入理解光学变迹函数以及ＦＴＳ的仪器函数这两个傅立叶变换光谱仪中的重要概念具有积极的意义。     

稀土化合物HoAl2.8Si0.2晶体结构测定

用Ｘ射线粉末衍射法测定ＨｏＡｌ２．８Ｓｉ．０２的晶体结构。该化合物属于三方晶系，在５００℃状态下，点阵参数用六方晶胞表示为：ａ＝６．１１２，ｃ＝２０．９２，ｃ／ａ＝３．４２３，空间群为，每个晶胞含９个化合式量，该化合物是由９层原子堆垛而成，其中９个Ｈｏ原子占据３（ａ）和以６（ｃ）位置，原子参数为ｚｃ＝２／９，Ａｌ和Ｓｉ原子可以互相替代，它们占据９（ｅ）和１８（ｈ）位置，原子参数为Ｘｈ＝１／２和Ｚｈ＝２／９．     

Fourier变换的改进形式--分数傅立叶变换

分数Fourier变换是对经典Fourier变换的改进,在处理非平稳信号时效果明显,且具有很好的可重构性。本文介绍了分数Fourier变换FRFT的定义、性质及变换图像的物理意义。     

Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH

Acid-sensing ion channels (ASICs) are voltage-independent, proton-activated receptors that belong to the epithelial sodium channel/degenerin family of ion channels and are implicated in perception of pain, ischaemic stroke, mechanosensation, learning and memory. Here we report the low-pH crystal structure of a chicken ASIC1 deletion mutant at 1.9 A resolution. Each subunit of the chalice-shaped homotrimer is composed of short amino and carboxy termini, two transmembrane helices, a bound chloride ion and a disulphide-rich, multidomain extracellular region enriched in acidic residues and carboxyl-carboxylate pairs within 3 A, suggesting that at least one carboxyl group bears a proton. Electrophysiological studies on aspartate-to-asparagine mutants confirm that these carboxyl-carboxylate pairs participate in proton sensing. Between the acidic residues and the transmembrane pore lies a disulphide-rich 'thumb' domain poised to couple the binding of protons to the opening of the ion channel, thus demonstrating that proton activation involves long-range conformational changes.     

快速傅立叶变换(EFT)的另一种推导方法及实现

快速傅立叶变换(FFT)改进了离散傅立叶变换(DFT)的计算过程,因其计算速度更为高效,被广泛运用于数字信号的实时处理中.本文从整数的进制表示形式阐述了基2FFT和基4FFT的原理,给出了相关推导及部分重要结论的证明.最后分别给出了迭代方程式及实现方法.相应的结论也适应于更高维的FFT变换中.