Key Structural Features (key + structural_feature)

Distribution by Scientific Domains


Selected Abstracts


THE ECONOMICS OF THE NON-DISTRIBUTION CONSTRAINT: A CRITICAL REAPPRAISAL

ANNALS OF PUBLIC AND COOPERATIVE ECONOMICS, Issue 1 2008
Vladislav VALENTINOV
ABSTRACT,:,This paper re-examines the non-distribution constraint as a key structural feature of non-profit organization. It argues that its traditional understanding as a trustworthiness-enhancing device is incomplete. This paper shows that the non-distribution constraint is also a reflection of the directly utility-enhancing character of involvement in non-profit firms for their key stakeholders. This alternative explanation allows one to solve the central puzzle of trustworthiness theory: why doesn't the non-distribution constraint destroy entrepreneurial motivation? Additionally, it helps one to understand the role of the non-distribution constraint in economic theories of non-profit organization that do not rely on trustworthiness theory. Finally, it enables one to logically integrate the different economic theories of non-profit organization. [source]


Structure of Arabidopsis chloroplastic monothiol glutaredoxin AtGRXcp

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 6 2010
Lenong Li
Monothiol glutaredoxins (Grxs) play important roles in maintaining redox homeostasis in living cells and are conserved across species. Arabidopsis thaliana monothiol glutaredoxin AtGRXcp is critical for protection from oxidative stress in chloroplasts. The crystal structure of AtGRXcp has been determined at 2.4, resolution. AtGRXcp has a glutaredoxin/thioredoxin-like fold with distinct structural features that differ from those of dithiol Grxs. The structure reveals that the putative active-site motif CGFS is well defined and is located on the molecular surface and that a long groove extends to both sides of the catalytic Cys97. Structural comparison and molecular modeling suggest that glutathione can bind in this groove and form extensive interactions with conserved charged residues including Lys89, Arg126 and Asp152. Further comparative studies reveal that a unique loop with five additional residues adjacent to the active-site motif may be a key structural feature of monothiol Grxs and may influence their function. This study provides the first structural information on plant CGFS-type monothiol Grxs, allowing a better understanding of the redox-regulation mechanism mediated by these plant Grxs. [source]


Optimization of the Azobenzene Scaffold for Reductive Cleavage by Dithionite; Development of an Azobenzene Cleavable Linker for Proteomic Applications

EUROPEAN JOURNAL OF ORGANIC CHEMISTRY, Issue 23 2010
Geoffray Leriche
Abstract In this paper we conducted an extensive reactivity study to determine the key structural features that favour the dithionite-triggered reductive cleavage of the azo,arene group. Our stepwise investigation allowed identification of a highly reactive azo,arene structure 25 bearing a carboxylic acid at the ortho position of the electron-poor arene and an ortho - O -alkyl-resorcinol as the electron-rich arene. Based on this 2-(2,-alkoxy-4,-hydroxyphenylazo)benzoic acid (HAZA) scaffold, the orthogonally protected difunctional azo,arene cleavable linker 26 was designed and synthesized. Selective linker deprotection and derivatization was performed by introducing an alkyne reactive group and a biotin affinity tag. This optimized azo,arene cleavable linker led to a total cleavage in less than 10 s with only 1 mM dithionite. Similar results were obtained in biological media. [source]


New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins

PIGMENT CELL & MELANOMA RESEARCH, Issue 6 2009
Concepcion Olivares
Summary Tyrosinases are widely distributed in nature. They are copper-containing oxidases belonging to the type 3 copper protein family, together with catechol oxidases and haemocyanins. Tyrosinases are essential enzymes in melanin biosynthesis and therefore responsible for pigmentation of skin and hair in mammals, where two more enzymes, the tyrosinase-related proteins (Tyrps), participate in the pathway. The structure and catalytic mechanism of mammalian tyrosinases have been extensively studied but they are not completely understood because of the lack of information on the tertiary structure. The availability of crystallographic data of one plant catechol oxidase and one bacterial tyrosinase has improved the model of the three-dimensional structure of the active site of the enzyme. Furthermore, sequence comparison of tyrosinase and the Tyrps reveals that the three orthologue proteins share many key structural features, because of their common origin from an ancestral gene, although the specific residues responsible for their different catalytic capabilities have not been identified yet. This review summarizes our current knowledge of tyrosinase and Tyrps structure and function and describes the catalytic mechanism of tyrosinase and Dct/Tyrp2, which are better characterized. [source]


Design and Synthesis of Cyclopeptide Analogues of the Potent Histone Deacetylase Inhibitor FR235222

CHEMMEDCHEM, Issue 10 2007
Luigi Gomez-Paloma Prof.
Abstract Various structurally modified analogues of FR235222 (1), a natural tetrapeptide inhibitor of mammalian histone deacetylases, were prepared in a convergent approach. The design of the compounds was aimed to investigate the effect of structural modifications of the tetrapeptide core involved in enzyme binding in order to overcome some synthetic difficulties connected with the natural product 1. The modifications introduced could also help identify key structural features involved in the mechanism of action of these compounds. The prepared molecules were subjected to in,vitro pharmacological tests, and their potency was tested on cultured cells. Two of the components of the array were found to be more potent than the parent compound 1 and almost as efficient as trichostatin,A (TSA). These results demonstrate that it is possible to synthesize highly active cyclic tetrapeptides using commercially available amino acids (with the exception of 2-amino-8-oxodecanoic acid, Ahoda). The nature of the residue in the second position of the cyclic peptide and the stereochemistry of the Ahoda tail are important for the inhibitory activity of this class of cyclic tetrapeptide analogues. [source]