![]() N,N',N''-三乙酰基壳三糖结构式
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常用名 | N,N',N''-三乙酰基壳三糖 | 英文名 | N,N',N''-Triacetylchitotriose |
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CAS号 | 38864-21-0 | 分子量 | 627.593 | |
密度 | 1.5±0.1 g/cm3 | 沸点 | 1146.9±65.0 °C at 760 mmHg | |
分子式 | C24H41N3O16 | 熔点 | 271-272ºC dec. | |
MSDS | 美版 | 闪点 | 647.4±34.3 °C |
Site-directed selection of oligonucleotide antagonists by competitive elution.
Antisense Nucleic Acid Drug Dev. 9(1) , 1-11, (1999) Oligonucleotide ligands that bind a protein or a small molecule of interest are readily isolated by in vitro selection and amplification of rare sequences from combinatorial libraries of sequence-randomized oligonucleotides (Gold et al., 1995). Classic system... |
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Kinetic analysis of barley chitinase.
Arch. Biochem. Biophys. 344 , 335-342, (1997) The endochitinase from barley is the archetypal enzyme for a large class of plant-derived antifungal chitinases. The X-ray structure was solved previously in our laboratory and a mechanism of action proposed based on structural considerations. In this manuscr... |
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Structure of full-length class I chitinase from rice revealed by X-ray crystallography and small-angle X-ray scattering.
Proteins 78(10) , 2295-305, (2010) The rice class I chitinase OsChia1b, also referred to as RCC2 or Cht-2, is composed of an N-terminal chitin-binding domain (ChBD) and a C-terminal catalytic domain (CatD), which are connected by a proline- and threonine-rich linker peptide. Because of the abi... |
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Crystal structures of Urtica dioica agglutinin and its complex with tri-N-acetylchitotriose.
J. Mol. Biol. 297(3) , 673-81, (2000) Urtica dioica agglutinin is a small plant lectin that binds chitin. We purified the isolectin VI (UDA-VI) and crystal structures of the isolectin and its complex with tri-N-acetylchitotriose (NAG3) were determined by X-ray analysis. The UDA-VI consists of two... |
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The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge.
J. Mol. Biol. 295(5) , 1275-88, (2000) The effects of lacking a specific disulfide bridge on the transition state in folding were examined in order to explore the folding-unfolding mechanism of lysozyme. Four species of three-disulfide variant of hen lysozyme (3SS-lysozyme) were prepared by replac... |
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Suppression of lysozyme aggregation at alkaline pH by tri-N-acetylchitotriose.
Biochim. Biophys. Acta 1794(6) , 913-20, (2009) Inhibiting protein misfolding and aggregation is imperative for treatment of amyloid diseases. In this regard small molecules which bind to and stabilize the monomeric protein have invited attention owing to their ability to significantly slow down or inhibit... |
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Toward the understanding of the structure and dynamics of protein-carbohydrate interactions: molecular dynamics studies of the complexes between hevein and oligosaccharidic ligands.
Carbohydr. Res. 339(5) , 985-94, (2004) Herein we study, through all atom molecular dynamics simulations, the complex between hevein and two N-acetylated chitin oligomers, namely N,N(')-diacetylchitobiose and N,N('),N(")-triacetylchitotriose. The results of the simulations for two disaccharide comp... |
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Solution- and bound-state conformational study of N,N',N"-triacetyl chitotriose and other analogous potential inhibitors of hevamine: application of trNOESY and STD NMR spectroscopy.
Chemistry 9(9) , 1964-73, (2003) The solution-state conformations of N,N',N"-triacetyl chitotriose (1) and other potential chitinase inhibitors 2-4 were studied using a combination of NMR spectroscopy (NOESY) and molecular mechanics calculations. Determination solely of the global energy min... |
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Characterization of glycosyl hydrolase family 3 beta-N-acetylglucosaminidases from Thermotoga maritima and Thermotoga neapolitana.
J. Biosci. Bioeng. 108(6) , 455-9, (2009) The genes encoding beta-N-acetylglucosaminidase (nagA and cbsA) from Thermotoga maritima and Thermotoga neapolitana were cloned and expressed in Escherichia coli in order to investigate whether Thermotoga sp. is capable of utilizing chitin as a carbon source.... |
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Characterisation by triple-quantum filtered 17O-NMR of water molecules buried in lysozyme and trapped in a lysozyme-inhibitor complex.
Biophys. Chem. 77(2-3) , 111-21, (1999) Triple-quantum filtering NMR sequences were used to study the multiexponential relaxation behaviour of H2 17O in the presence of hen egg white lysozyme. By this means, the fraction and the correlation time of water were determined in slow motion, as well as t... |