Synthesis and biomedical applications of glycopolymers.

On the nature of unique boron sites in borate glasses

Irrational tilt grain boundaries as one-dimensional quasicrystals

Previously it was shown that the nuclear envelope-limited sheets of chromatin, monolayers of nucleoprotein structural units, are present in blood cells from 4 classes of vertebrates. Now we show that sheets of similar width are present in certain leukocytes of a fifth class, a teleost fish. We describe the fine structure of leukocytes in peripheral blood and in the main haematopoietic organ, kidney. We also examined the granulocytes of connective tissue in intestine. By May-Grunwald-Giemsa staining and electron microscopy heterophilic granulocytes, cosinophils but no basophils could be recognized in peripheral blood and kidney. Problems in classification of the cells are discussed. In one group (A) of 5 fish, sheets occurred at a frequency of roughly 1% in heterophilic (type 1) granulocytes and lymphocytes from peripheral blood. No sheets were found in a second group (B) of 5 fish. Kidney and intestine were examined in some fish from both groups and no sheets were present. In an atypical group (C) sheets were found in the eosinophilic (type 2) granulocytes from peripheral blood of one fish and in lymphocytes from connective tissue of intestine in another. Sheets were usually associated with nuclei of irregular shape and their width averaged 36 nm. We tabulate data from other workers on occurence and width of sheets. They are found in all the main classes of tissue in mammals, namely blood and other connective tissues, in epithelial, nervous, germinal tissue and muscle, as well as in invertebrate and certain plants. Their nearly constant width, average value 35 nm, provides very convincing evidence for the hypothesis that the molecules of DNA and protein are organized into the same fundamental structural units, irrespective of species. We discuss the variable incidence of sheets among different cell types and the factors which might determine this.

本文从点阵间隔、密度以及衍射强度的测量详尽地研究了Al-Ni合金在δ相区内的结构变化。点阵间隔的量度表明:在不到4原子百分数的狭隘均匀范围内,α和c初则随Ni含量的增加而递减,过理想成分Ni2Al3以后,则又随Ni含量的增加而递增;也就是说,α和c在理想成分处同时出现最小值。密度和衍射强度的数据无可辩驳地指出这样一个事实:当Ni含量少于理想成分时,每晶胞所含的原子数恒为5,Al原子无规地替代了在赝立方体心位置上的部分Ni原子;当Ni含量超出理想成分时,每晶胞所含的原子数多于5,多余的Ni原子无规地填充到原来在理想结构中所空出的部分体心位置上去。决定这些变化的主要困素是基本结构单位内所含的平均价电子数,在δ相区内,每基本结构单位即每赝立方体的平均价电子数不能小于3。δ相和同一系统中的β相适成互补的对应关系,它是合金相缺陷点阵的一种新类型。

Molecular dynamics simulations of 45° [100] twist plus tilt grain boundaries in aluminum

Coarse-grained mechanical models for viral capsids

We have studied the amorphization process of SnI4 up to 26.8 GPa with unprecedented experimental details by combining Sn and I K-edge x-ray absorption spectroscopy and powder x-ray diffraction. Standard and reverse Monte Carlo extended x-ray absorption fine structure (EXAFS) refinements confirm that the penta atomic SnI4 structural unit tetrahedron is a fundamental structural unit that appears preserved through the crystalline phase-I to crystalline phase-II transition that has been previously reported between 7 GPa and 10 GPa. Up to now, unexploited iodine EXAFS reveals to be extremely informative and confirms the progressive formation of iodine-iodine short bonds close to 2.85 Å. A coordination number increase of Sn in the crystalline phase-II region appears to be excluded, while the deformation of the tetrahedral units proceeds through a flattening that keeps the average I-Sn-I angle close to 109.5°. Moreover, we put in evidence the impact of pressure on the Sn near edge structure under competing geometrical and electronic effects.

Review: 79 refs.

Bioactive benzofuran derivatives: moracins A-Z in medicinal chemistry.

Internal repeats are widely found in proteins and considered to be important in protein evolution and function. Three major types of internal repeat including domain, solenoid, and fibrous repeats are shown in Figure 1. These repeats may involve in protein-protein interaction as well as binding to various ligands such as DNA and RNA. For example, the tetratrico peptide repeats (TPR) that are involved in cell-cycle regulation, transcriptional regulation, protein transport, and assisting protein folding [1][2], and the TATA-binding protein (TBP) is a transcription factor that binds specifically to a DNA sequence [3]. To identify and classify various types of protein repeats with different lengths from a query protein sequence or structure, we have designed a comprehensive system which focuses on analyzing autocorrelation relationships of sequence contents and topology of secondary structures within a protein. A complete database containing verified fundamental repeat sequence peptides and structural units for homologous matching analysis is also constructed. The data flow diagram of the proposed identification system is shown in Figure 2, which contains two major parts: Repeat Database and Internal Repeat Analyzer. The Repeat Database is constructed by evaluating proteins from SCOP and Pfam through an autocorrelation mechanism. The Internal Repeat Analyzer is designed as a three-level hierarchical analysis for detecting domain, solenoid, and fibrous repeat respectively. In addition, an iteratively refined multiple structure alignment tool has been developed for comparing and verifying those extracted internal repeat substructures. In this study, the collected database contains 162 domain families with repeat chatacteristics, 28 fundamental repeat structure units and 129 repeat subsequences retrieved from 1,961 superfamilies, and we have demonstrated the proposed system can efficiently identify repeat topologies of proteins.

Tremendous progress and innovation has ushered the incorporation of semiconducting single-walled carbon nanotubes (s-SWCNTs) as active components into organic/inorganic/hybrid solar cells and thermoelectrics. For solar photoconversion, strong and tunable absorption is necessitated, suggesting that s-SWCNTs can play a role as light-harvesting components, however the narrow and distinct excitonic optical transitions found in s-SWCNT systems limit broad-band absorption. As such, we introduce encapsulation of small molecules within the endohedral volume of s-SWCNTs as a route to increase and extend light absorption in regions outside s-SWCNT excitonic transitions. Creation of this self-assembled supra-molecular system can strongly modify the opto-electronic properties of both the s-SWCNT and encapsulated molecule. We investigate excitation energy transfer occurring from encapsulated dye molecules to s-SWCNTs, which results in luminescent SWCNT excitons. We exploit the high-throughput and chiral selectivity of polyfluorene wrapping methods to generate dispersions of s-SWCNTs with dye encapsulation. We demonstrate that the selectivity of the polyfluorene polymer for semiconducting chiral distributions is not affected by the presence of encapsulated molecules. Tracking the excited state transient absorption signatures of excitation energy transfer provides detailed information regarding dynamics of both the encapsulated dye and s-SWCNTs. We observe sub-picosecond excitation energy transfer of excitons generated in dye molecules to the surrounding s-SWCNTs. Photoluminescence excitation maps reveal that the absorption of encapsulated dye molecules depends sensitively on the diameter of the s-SWCNT in which they are encapsulated. We consider a simple molecular exciton model to describe aggregate formation within the s-SWCNT endohedral volume, which reveals that the dye molecules adopt unique aggregate structures that are defined both by a competition between intermolecular interactions between the dye molecules and confinement effects due to the s-SWCNT diameter. Small molecule encapsulation in s-SWCNTs serves as a strong platform to control intermolecular interactions in small molecule systems through confinement, which opens up the possibility of enhancing photo-induced extraction of energy and charge in s-SWCNTs solar photoconversion systems.

Colloidosomes constructed by the self-assembly of nanoparticles (NPs) on liquid–liquid interfaces have been demonstrated to be useful in many fields. However, the interspaces between NPs on the surface of colloidosomes barricade their application in small molecule encapsulation. Herein, fabrication of a new type of colloidosome built by the seamless connection of NPs via simply heating and quenching a type of core–shell structured NPs (CSNPs) aqueous system using oil as a template, is presented. These colloidosomes have a hollow structure and exhibit efficient small molecule encapsulation. More importantly, the colloidosomes can dissociate into single NPs and release the small target molecules encapsulated in interior of the colloidosomes at a temperature higher than the melting point of the CSNP shell. It is also shown that the dissociation temperature of colloidosomes can be controlled by simply adjusting the length of the PEG chains in the CSNP shell, which implies that these intelligent capsules have attractive application prospects in controlled drug release.

Initial attempts to correlate the distribution of gene density (number of gene loci per unit length on the linkage map) with the distribution of lengths of coding sequences have led to the observation that 46% of approximately 1000 sampled proteins in Escherichia coli have molecular masses of n X 14,000 +/- 2500 daltons (n = 1, 2, ...). This clustering around multiples of 14,000 contrasts with the 36% one would expect in these ranges if the sizes were uniformly distributed. The entire distribution is well fit by a sum of normal or lognormal distributions located at multiples of 14,000, which suggests that the percentage of E. coli proteins governed by the underlying sizing mechanism is much greater than 50%. Clustering of protein molecular sizes around multiples of a unit size also is suggested by the distribution of well-characterized HeLa cell proteins. The distribution of gene lengths for E. coli suggests regular clustering, which implies that the clustering of protein molecular masses is not an artifact of the molecular mass measurement by gel electrophoresis. These observations suggest the existence of a fundamental structural unit. The rather uniform size of this structural unit (without any apparent sequence homology) suggests that a general principle such as geometrical or physical optimization at the DNA or protein level is responsible. This suggestion is discussed in relation to experimental evidence for the domain structure of proteins and to existing hypotheses that attempt to account for these domains. Microevolution would appear to be accommodated by incremental changes within this fundamental unit, whereas macroevolution would appear to involve "quantum" changes to the next stable size of protein.

The Queensway folds are an anticline–syncline pair in layered limestone and shale of the Ottawa Formation in the Ottawa – St. Lawrence Lowlands. They are parallel, flexural-slip folds with horizontal axes trending northwest, parallel to the surface trace of the Gloucester fault.Five principal fracture subpatterns were recognized in the fold-pair, caused by at least four geometrically distinct stress fields. The principal stress directions at failure for all five subpatterns coincided, moreover, with the three orthogonal fabric axes, and the maximum principal stress was either parallel or perpendicular to the fold axes and to the Gloucester fault.Slickenside striae on bedding and on fractures at an angle to bedding indicate two principal kinematic patterns in the fold-pair; the one arises from motion in the deformation plane as a consequence of the folding and the other from strike-slip motion perpendicular to that plane as a consequence of displacement on the Gloucester fault.Slickensides indicate that each bed was free to move relative to adjacent ones during folding and that the fundamental structural unit in flexural-slip folding is the bed. Model studies support the field data and indicate that the sense and magnitude of interbed slip in any structural position is dependent upon an integral of conditions throughout the fold-pair and that the fundamental fold unit is the anticline–syncline pair.

The proper function of the genome largely depends on the higher-order architecture of the chromosome. To understand the detailed chromosome structure in a native state, we developed an on-substrate procedure of subcellular fractionation suitable for the observation by atomic force microscopy (AFM). HeLa cells on a coverslip were successively treated with a detergent and a high-salt solution to remove the cytoplasmic and nucleoplasmic materials. A closer observation of the nucleus by AFM revealed that the interphase chromosome is composed of a granular unit of approximately 80 nm in diameter. Subsequent mild treatment with deoxyribonuclease I (10 U ml(-1)) exposed these units more clearly, which enabled us to uncover the 80-nm granules forming a fibre of approximately 80 nm width. In the cytoplasmic regions, cytoskeletal fibres with varying widths (10-70 nm) were observed. These observations suggest that the 80 nm granular fibre is a fundamental structural unit of the interphase chromosome. This on-substrate procedure was also applied to Escherichia coli. Cells attached on a coverslip were successively treated with lysozyme and detergent to partially release the nucleoid onto the substrate. The AFM observation revealed that the approximately 80 nm fundamental structural unit forms a granular fibre similar to that of HeLa cells. These results suggest that the fundamental mechanism of chromosome packing is common in both prokaryotes and eukaryotes.