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Multiple Substitutions (multiple + substitution)

Distribution by Scientific Domains

Chemistry	80%

Selected Abstracts

The new ternary phases of La3(Zn0.874Mg0.126)11 and Ce3(Zn0.863Mg0.137)11

ACTA CRYSTALLOGRAPHICA SECTION C, Issue 3 2010
Volodymyr Pavlyuk
The new ternary intermetallic title compounds, namely trilanthanum undeca(zinc/magnesium), La3(Zn0.874Mg0.126)11, (I), and tricerium undeca(zinc/magnesium), Ce3(Zn0.863Mg0.137)11, (II), are isostructural and crystallize in the orthorhombic La3Al11 structure type. These three phases belong to the same structural family, the representative members of which may be derived from the tetragonal BaAl4 structure type by a combination of internal deformation and multiple substitution. Compared to the structure of La3Al11, in (I), a significant decrease of 11.9% in the unit-cell b axis and an increase in the other two directions, of 3.6% along a and 5.2% along c, are observed. Such an atypical deformation is caused by the closer packing of atoms in the unit cell due to atom shifts that reflect strengthening of metallic-type bonding. This structural change is also manifested in a significant difference in the coordination around the smaller atoms at the 8l Wyckoff position (site symmetry m). The Al atom in La3Al11 is in a tricapped trigonal prismatic environment (coordination number 9), while the Zn atoms in (I) and (II) are situated in a tetragonal antiprism with two added atoms (coordination number 10). [source]

A general method to prepare monodentate phosphane ligands with mixed substituents

HETEROATOM CHEMISTRY, Issue 7 2009
Jennifer E. Phelps
Treatment of (2,2,-biphenylylene)- phosphorchloridite ester [(C12H8O2)PCl] (1) with C2F5Li yields (C12H8O2)PC2F52; treatment of 1 with Grignard reagents yields compounds of the type (C12H8O2)PR (R = iPr, 5; Et 6). In both cases, the 1,3-dioxepine ring formed when 2,2,-biphenol reacts with PCl3 to form 1 serves as a protecting group at the phosphorus atom; the ring allows the stepwise introduction of one substituent and prevents undesirable product mixtures associated with multiple substitutions at the phosphorus. Additional treatment of compounds 2, 5, and 6 with Grignard, alkyl-, or aryllithium reagents results in the formation of unsymmetrically substituted phosphanes. The use of (2,2,-biphenylylene)phosphorchloridite ester as a starting material for the preparation of electroneutral phosphanes of the type (Rf)PR2 and electron-poor phosphanes of the type (Rf)2PR is described. © 2010 Wiley Periodicals, Inc. Heteroatom Chem 20:393,397, 2009; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/hc.20563 [source]

An efficient algorithm for multistate protein design based on FASTER

JOURNAL OF COMPUTATIONAL CHEMISTRY, Issue 5 2010
Benjamin D. Allen
Abstract Most of the methods that have been developed for computational protein design involve the selection of side-chain conformations in the context of a single, fixed main-chain structure. In contrast, multistate design (MSD) methods allow sequence selection to be driven by the energetic contributions of multiple structural or chemical states simultaneously. This methodology is expected to be useful when the design target is an ensemble of related states rather than a single structure, or when a protein sequence must assume several distinct conformations to function. MSD can also be used with explicit negative design to suggest sequences with altered structural, binding, or catalytic specificity. We report implementation details of an efficient multistate design optimization algorithm based on FASTER (MSD-FASTER). We subjected the algorithm to a battery of computational tests and found it to be generally applicable to various multistate design problems; designs with a large number of states and many designed positions are completely feasible. A direct comparison of MSD-FASTER and multistate design Monte Carlo indicated that MSD-FASTER discovers low-energy sequences much more consistently. MSD-FASTER likely performs better because amino acid substitutions are chosen on an energetic basis rather than randomly, and because multiple substitutions are applied together. Through its greater efficiency, MSD-FASTER should allow protein designers to test experimentally better-scoring sequences, and thus accelerate progress in the development of improved scoring functions and models for computational protein design. © 2009 Wiley Periodicals, Inc. J Comput Chem, 2010 [source]

TBP domain symmetry in basal and activated archaeal transcription

MOLECULAR MICROBIOLOGY, Issue 1 2009
Mohamed Ouhammouch
Summary The TATA box binding protein (TBP) is the platform for assembly of archaeal and eukaryotic transcription preinitiation complexes. Ancestral gene duplication and fusion events have produced the saddle-shaped TBP molecule, with its two direct-repeat subdomains and pseudo-two-fold symmetry. Collectively, eukaryotic TBPs have diverged from their present-day archaeal counterparts, which remain highly symmetrical. The similarity of the N- and C-halves of archaeal TBPs is especially pronounced in the Methanococcales and Thermoplasmatales, including complete conservation of their N- and C-terminal stirrups; along with helix H,1, the C-terminal stirrup of TBP forms the main interface with TFB/TFIIB. Here, we show that, in stark contrast to its eukaryotic counterparts, multiple substitutions in the C-terminal stirrup of Methanocaldococcus jannaschii (Mja) TBP do not completely abrogate basal transcription. Using DNA affinity cleavage, we show that, by assembling TFB through its conserved N-terminal stirrup, Mja TBP is in effect ambidextrous with regard to basal transcription. In contrast, substitutions in either its N- or the C-terminal stirrup abrogate activated transcription in response to the Lrp-family transcriptional activator Ptr2. [source]

A new generation of protein display scaffolds for molecular recognition

PROTEIN SCIENCE, Issue 1 2006
Ralf J. Hosse
Abstract Engineered antibodies and their fragments are invaluable tools for a vast range of biotechnological and pharmaceutical applications. However, they are facing increasing competition from a new generation of protein display scaffolds, specifically selected for binding virtually any target. Some of them have already entered clinical trials. Most of these nonimmunoglobulin proteins are involved in natural binding events and have amazingly diverse origins, frameworks, and functions, including even intrinsic enzyme activity. In many respects, they are superior over antibody-derived affinity molecules and offer an ever-extending arsenal of tools for, e.g., affinity purification, protein microarray technology, bioimaging, enzyme inhibition, and potential drug delivery. As excellent supporting frameworks for the presentation of polypeptide libraries, they can be subjected to powerful in vitro or in vivo selection and evolution strategies, enabling the isolation of high-affinity binding reagents. This article reviews the generation of these novel binding reagents, describing validated and advanced alternative scaffolds as well as the most recent nonimmunoglobulin libraries. Characteristics of these protein scaffolds in terms of structural stability, tolerance to multiple substitutions, ease of expression, and subsequent applications as specific targeting molecules are discussed. Furthermore, this review shows the close linkage between these novel protein tools and the constantly developing display, selection, and evolution strategies using phage display, ribosome display, mRNA display, cell surface display, or IVC (in vitro compartmentalization). Here, we predict the important role of these novel binding reagents as a toolkit for biotechnological and biomedical applications. [source]