Solvent‐Enhanced Conformational Flexibility of Cyclic Tetrapeptides

Author(s):  
Nadja Berger ◽  
Laura J. B. Wollny ◽  
Pandian Sokkar ◽  
Sumit Mittal ◽  
Joel Mieres‐Perez ◽  
...  
ChemPhysChem ◽  
2019 ◽  
Vol 20 (13) ◽  
pp. 1661-1661
Author(s):  
Nadja Berger ◽  
Laura J. B. Wollny ◽  
Pandian Sokkar ◽  
Sumit Mittal ◽  
Joel Mieres-Perez ◽  
...  

ChemPhysChem ◽  
2019 ◽  
Vol 20 (13) ◽  
pp. 1663-1663
Author(s):  
Nadja Berger ◽  
Laura J. B. Wollny ◽  
Pandian Sokkar ◽  
Sumit Mittal ◽  
Joel Mieres-Perez ◽  
...  

2016 ◽  
pp. n/a-n/a
Author(s):  
Shu-quan Li ◽  
Ya-bin Yang ◽  
Xue-qiong Yang ◽  
Yi Jiang ◽  
Zhen-jie Li ◽  
...  
Keyword(s):  

1988 ◽  
Vol 53 (5) ◽  
pp. 889-902
Author(s):  
Josef Šebek

It is shown that the formation of the so-called rotator phase of alkanes (one of the high temperature crystalline phases) might be connected with a partial increase of the conformational flexibility of chains. The conformations with higher number of kinks per chain, which have been neglected till now, are shown to contribute effectively to the conformational partition function. Small probability of these states given by the Boltzmann exponent is compensated by a large number of ways in which they can be distributed along the chain. The deduced features of the rotator phase seem to be in agreement with the experimentally observed properties.


2021 ◽  
Vol 21 (2) ◽  
pp. 897-907
Author(s):  
Giovanni Pierri ◽  
Marta Corno ◽  
Eleonora Macedi ◽  
Maria Voccia ◽  
Consiglia Tedesco

2021 ◽  
Vol 22 (6) ◽  
pp. 3012
Author(s):  
James I. Mitchell-White ◽  
Thomas Stockner ◽  
Nicholas Holliday ◽  
Stephen J. Briddon ◽  
Ian D. Kerr

The five members of the mammalian G subfamily of ATP-binding cassette transporters differ greatly in their substrate specificity. Four members of the subfamily are important in lipid transport and the wide substrate specificity of one of the members, ABCG2, is of significance due to its role in multidrug resistance. To explore the origin of substrate selectivity in members 1, 2, 4, 5 and 8 of this subfamily, we have analysed the differences in conservation between members in a multiple sequence alignment of ABCG sequences from mammals. Mapping sets of residues with similar patterns of conservation onto the resolved 3D structure of ABCG2 reveals possible explanations for differences in function, via a connected network of residues from the cytoplasmic to transmembrane domains. In ABCG2, this network of residues may confer extra conformational flexibility, enabling it to transport a wider array of substrates.


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