scholarly journals Total structure determination of surface doping [Ag46Au24(SR)32](BPh4)2 nanocluster and its structure-related catalytic property

2015 ◽  
Vol 1 (7) ◽  
pp. e1500441 ◽  
Author(s):  
Shuxin Wang ◽  
Shan Jin ◽  
Sha Yang ◽  
Shuang Chen ◽  
Yongbo Song ◽  
...  
Keyword(s):  
Surface Structure ◽  
Catalytic Property ◽  
Surface Characterization ◽  
Structure Effect ◽  
Crystallographic Structure ◽  
X Ray ◽  
First Case ◽  
Basic Understanding ◽  
Total Structure

The structure effect is widely present in the catalysis of alloy systems. However, the surface structure of this system is still ambiguous because of the limitations of the current surface characterization tools. We reported the x-ray crystallographic structure of the first and the largest AgAu alloy nanocluster with a doping shell formulated as [Ag46Au24(SR)32](BPh4)2. This nanocluster consists of an achiral bimetallic Ag2@Au18@Ag20 core protected by a chiral Ag24Au6(SR)32 shell. The catalysis experiments further revealed that the surface structure affects the selectivity of products significantly. This is the first case to find the structure effect in atomically precise alloy nanoclusters. Our work will benefit the basic understanding of bimetal distribution, as well as the structure-related catalytic property of alloy nanoclusters at the atomic level.

scholarly journals X-ray crystallographic structure determination of the smoke-derived karrikin KAR3

2013 ◽  
Vol 88 ◽  
pp. 107-109 ◽  
Author(s):  
J.J. Nair ◽  
O.Q. Munro ◽  
M. Pošta ◽  
H.B. Papenfus ◽  
P. Beier ◽  
...  
Keyword(s):  
Structure Determination ◽  
Crystallographic Structure ◽  
X Ray

The amino acid sequence of yeast phosphoglycerate mutase

1982 ◽  
Vol 215 (1198) ◽  
pp. 19-44 ◽  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Proteolytic Enzymes ◽  
Phosphoglycerate Mutase ◽  
Crystallographic Structure ◽  
X Ray ◽  
C Terminus ◽  
Detailed Interpretation ◽  
High Degree

The complete amino acid sequence of yeast phosphoglycerate mutase comprising 241 residues has been determined. The sequence was deduced from the two cyanogen bromide fragments, and from the peptides derived from these fragments after digestion by a number of proteolytic enzymes. Determination of this sequence now allows a detailed interpretation of the existing high-resolution X-ray crystallographic structure. A comparison of the sequence reported here with the sequences of peptides from phosphoglycerate mutases from other species, and with the sequence of erythrocyte diphosphoglycerate mutase, indicates that these enzymes have a high degree of structural homology. Autolysis of phosphoglycerate mutase by yeast extracts leads to the complete loss of mutase activity, and the formation of electrophoretically distinguishable forms (R. Sasaki, E. Sugimoto & H. Chiba, Archs Biochem. Biophys. 115, 53-61 (1966)). It is apparent from the amino acid sequence that these changes are due to the loss of an 8─12 residue peptide from the C-terminus.

The synthesis and properties of two stable benzo[c]furans. An x-ray crystallographic structure determination of the geometry of 1-cyano-5,6-(methylenedioxy)benzo[c]furan

1986 ◽  
Vol 51 (21) ◽  
pp. 3973-3978 ◽  
Author(s):  
Russell Rodrigo ◽  
Susan M. Knabe ◽  
Nicholas J. Taylor ◽  
Dayananda Rajapaksa ◽  
Michael J. Chernishenko
Keyword(s):  
Structure Determination ◽  
Crystallographic Structure ◽  
X Ray

ChemInform Abstract: X-Ray Crystallographic Structure Determination of Some Unique Chiral Sultam Derivatives.

ChemInform ◽  
2010 ◽  
Vol 28 (24) ◽  
pp. no-no
Author(s):  
H. KAKUDA ◽  
T. SUZUKI ◽  
Y. TAKEUCHI ◽  
M. SHIRO
Keyword(s):  
Structure Determination ◽  
Crystallographic Structure ◽  
X Ray
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