scholarly journals Reversible α-helix formation controlled by a hydrogen bond surrogate

Tetrahedron ◽  
2012 ◽  
Vol 68 (23) ◽  
pp. 4434-4437 ◽  
Author(s):  
Stephen E. Miller ◽  
Neville R. Kallenbach ◽  
Paramjit S. Arora
2012 ◽  
Vol 134 (18) ◽  
pp. 8000-8000 ◽  
Author(s):  
Laura K. Henchey ◽  
Swati Kushal ◽  
Ramin Dubey ◽  
Ross N. Chapman ◽  
Bogdan Z. Olenyuk ◽  
...  

2010 ◽  
Vol 132 (23) ◽  
pp. 7868-7869 ◽  
Author(s):  
Li Guo ◽  
Aaron M. Almeida ◽  
Weicheng Zhang ◽  
Andrew G. Reidenbach ◽  
Soo Hyuk Choi ◽  
...  

2004 ◽  
Vol 126 (39) ◽  
pp. 12252-12253 ◽  
Author(s):  
Ross N. Chapman ◽  
Gianluca Dimartino ◽  
Paramjit S. Arora

2008 ◽  
Vol 130 (13) ◽  
pp. 4334-4337 ◽  
Author(s):  
Jie Liu ◽  
Deyun Wang ◽  
Qi Zheng ◽  
Min Lu ◽  
Paramjit S. Arora

2010 ◽  
Vol 132 (3) ◽  
pp. 941-943 ◽  
Author(s):  
Laura K. Henchey ◽  
Swati Kushal ◽  
Ramin Dubey ◽  
Ross N. Chapman ◽  
Bogdan Z. Olenyuk ◽  
...  

2007 ◽  
Vol 18 (01) ◽  
pp. 91-98 ◽  
Author(s):  
GÖKHAN GÖKOĞLU ◽  
TARIK ÇELİK

We have performed parallel tempering simulations of a 13-residue peptide fragment of ribonuclease-A, c-peptide, in implicit solvent with constant dielectric permittivity. This peptide has a strong tendency to form α-helical conformations in solvent as suggested by circular dichroism (CD) and nuclear magnetic resonance (NMR) experiments. Our results demonstrate that 5th and 8–12 residues are in the α-helical region of the Ramachandran map for global minimum energy state in solvent environment. Effects of salt bridge formation on stability of α-helix structure are discussed.


2014 ◽  
Vol 13 (3) ◽  
pp. 541 ◽  
Author(s):  
Elena V. Eremeeva ◽  
Ludmila P. Burakova ◽  
Vasilisa V. Krasitskaya ◽  
Alexander N. Kudryavtsev ◽  
Osamu Shimomura ◽  
...  

2021 ◽  
pp. 108007
Author(s):  
Eloise Masquelier ◽  
Sheng-Ping Liang ◽  
Lior Sepunaru ◽  
Daniel E. Morse ◽  
Michael J. Gordon
Keyword(s):  

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Lise Friis Christensen ◽  
Lasse Staby ◽  
Katrine Bugge ◽  
Charlotte O’Shea ◽  
Birthe B. Kragelund ◽  
...  

AbstractRadical-Induced Cell Death1 (RCD1) functions as a cellular hub interacting with intrinsically disordered transcription factor regions, which lack a well-defined three-dimensional structure, to regulate plant stress. Here, we address the molecular evolution of the RCD1-interactome. Using bioinformatics, its history was traced back more than 480 million years to the emergence of land plants with the RCD1-binding short linear motif (SLiM) identified from mosses to flowering plants. SLiM variants were biophysically verified to be functional and to depend on the same RCD1 residues as the DREB2A transcription factor. Based on this, numerous additional members may be assigned to the RCD1-interactome. Conservation was further strengthened by similar intrinsic disorder profiles of the transcription factor homologs. The unique structural plasticity of the RCD1-interactome, with RCD1-binding induced α-helix formation in DREB2A, but not detectable in ANAC046 or ANAC013, is apparently conserved. Thermodynamic analysis also indicated conservation with interchangeability between Arabidopsis and soybean RCD1 and DREB2A, although with fine-tuned co-evolved binding interfaces. Interruption of conservation was observed, as moss DREB2 lacked the SLiM, likely reflecting differences in plant stress responses. This whole-interactome study uncovers principles of the evolution of SLiM:hub-interactions, such as conservation of α-helix propensities, which may be paradigmatic for disorder-based interactomes in eukaryotes.


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