Order-order transition in a macromolecular system—poly-L-proline I and II

Pramana ◽  
1981 ◽  
Vol 17 (4) ◽  
pp. 361-368 ◽  
Author(s):  
R C Agnihotri ◽  
C Mehrotra ◽  
V D Gupta ◽  
Vandana Srivastava
Keyword(s):  
Order Transition ◽  
Macromolecular System

scholarly journals Deciphering the Role of Residues Involved in Disorder-To-Order Transition Regions in Archaeal tRNA Methyltransferase 5

Genes ◽  
2021 ◽  
Vol 12 (3) ◽  
pp. 399
Author(s):  
Ambuj Srivastava ◽  
Dhanusha Yesudhas ◽  
Shandar Ahmad ◽  
M. Michael Gromiha
Keyword(s):  
Three Dimensional ◽  
Md Simulations ◽  
Order Transition ◽  
Free Form ◽  
Wild Type ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Type Complex ◽  
In The Wild ◽  
Trna Methyltransferase

tRNA methyltransferase 5 (Trm5) enzyme is an S-adenosyl methionine (AdoMet)-dependent methyltransferase which methylates the G37 nucleotide at the N1 atom of the tRNA. The free form of Trm5 enzyme has three intrinsically disordered regions, which are highly flexible and lack stable three-dimensional structures. These regions gain ordered structures upon the complex formation with tRNA, also called disorder-to-order transition (DOT) regions. In this study, we performed molecular dynamics (MD) simulations of archaeal Trm5 in free and complex forms and observed that the DOT residues are highly flexible in free proteins and become stable in complex structures. The energetic contributions show that DOT residues are important for stabilising the complex. The DOT1 and DOT2 are mainly observed to be important for stabilising the complex, while DOT3 is present near the active site to coordinate the interactions between methyl-donating ligands and G37 nucleotides. In addition, mutational studies on the Trm5 complex showed that the wild type is more stable than the G37A tRNA mutant complex. The loss of productive interactions upon G37A mutation drives the AdoMet ligand away from the 37th nucleotide, and Arg145 in DOT3 plays a crucial role in stabilising the ligand, as well as the G37 nucleotide, in the wild-type complex. Further, the overall energetic contribution calculated using MMPBSA corroborates that the wild-type complex has a better affinity between Trm5 and tRNA. Overall, our study reveals that targeting DOT regions for binding could improve the inhibition of Trm5.

scholarly journals First Order Transition for the Optimal Search Time of Lévy Flights with Resetting

2014 ◽  
Vol 113 (22) ◽  
Author(s):  
Lukasz Kusmierz ◽  
Satya N. Majumdar ◽  
Sanjib Sabhapandit ◽  
Grégory Schehr
Keyword(s):  
Search Time ◽  
Order Transition ◽  
Optimal Search ◽  
Lévy Flights ◽  
First Order ◽  
Levy Flights ◽  
First Order Transition

Fluctuation-induced first-order transition in the Hubbard model

1990 ◽  
Vol 74 (11) ◽  
pp. 1175-1179 ◽  
Author(s):  
M.D. Coutinho-Filho ◽  
M.L. Lyra ◽  
A.M. Nemirovsky
Keyword(s):  
Hubbard Model ◽  
Order Transition ◽  
First Order ◽  
First Order Transition
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