Biologically active conformation of M-cholinolytic agents in the series of dialkylaminoalkyl esters of carboxylic acids and their structural analogs

1974 ◽  
Vol 8 (7) ◽  
pp. 403-405
Author(s):  
S. N. Golikov ◽  
S. G. Kuznetsov ◽  
S. M. Chigareva ◽  
M. I. Volkova
Keyword(s):  
Carboxylic Acids ◽  
Biologically Active ◽  
Active Conformation ◽  
Esters Of Carboxylic Acids ◽  
Cholinolytic Agents ◽  
Biologically Active Conformation

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
Keyword(s):  
Biologically Active ◽  
Active Conformation ◽  
X Ray ◽  
Biologically Active Conformation

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).

scholarly journals Analysis of the code relating sequence to conformation in globular proteins. Theory and application of expected information

1974 ◽  
Vol 141 (3) ◽  
pp. 853-867 ◽  
Author(s):  
Barry Robson
Keyword(s):  
Information Theory ◽  
Theoretical Basis ◽  
Biologically Active ◽  
Active Conformation ◽  
Primary Sequence ◽  
Theory Analysis ◽  
Expected Information ◽  
Transfer Of Information ◽  
Algebraic Formulation ◽  
Biologically Active Conformation

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).

Sign in / Sign up

Export Citation Format

Share Document