The determination of thymopoietin conformation based on X-ray structure of a discontinuous thymopoietin-like motif of G-actin.

1997 ◽  
Vol 44 (3) ◽  
pp. 519-525
Author(s):  
I Z Siemion ◽  
I Strug ◽  
Z Szewczuk

The biologically active conformation of thymopoietin, based on X-ray data reported for discontinuous thymopoietin-like motif of G-actin, is proposed. The conformation is compared with that resulting from the prediction made by the method of Chou & Fasman (Annu. Rev. Biochem. 47, 251-276, 1978) and Rost & Sander (Methods Enzymol. 266, 525-539, 1996).

1974 ◽  
Vol 141 (3) ◽  
pp. 853-867 ◽  
Author(s):  
Barry Robson

1. An information theory analysis of the folding of a globular protein is proposed. 2. The folding is seen as a transfer of information between two messages, the primary sequence and the biologically active conformation. 3. It is shown how the information transferred was estimated by inspection of proteins of known primary sequence and conformation. 4. In this estimation, concerted use of subjective (Bayesian) probabilities leads to a more robust approach which can be employed whether the number of proteins of known sequence and conformation is large or small. 5. Further, it is demonstrated that the problem then becomes a very simple algebraic formulation for information estimates. 6. Finally, it is shown how this process of information theory analysis can be reversed to predict the conformation of a protein by using its primary sequence and the above information estimates obtained from other proteins. 7. The present paper provides the theoretical basis for the derivation and application of a stereochemical alphabet (Robson & Pain, 1974a,c), and for an investigation of the effects of residues on the conformations of their neighbours (Robson & Pain, 1974b).


Molbank ◽  
10.3390/m1125 ◽  
2020 ◽  
Vol 2020 (2) ◽  
pp. M1125
Author(s):  
Yuichiro Kanno ◽  
Taichi Kusakabe ◽  
Nao Saito ◽  
Shoko Kikkawa ◽  
Keisuke Takahashi ◽  
...  

The palladium catalyzed carbonylation of 1 using the chiral ligand L1 afforded 2 in a highly diastereoselective manner. The stereochemistry of the major diastereomer 2a was determined by X-ray crystallographic analysis. AR luciferase reporter assay studies suggested that 2a was the active constituent of YK11 (2).


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