scholarly journals Weakly bound states with spin-isospin symmetry

2016 ◽  
Vol 113 ◽  
pp. 03001 ◽  
Author(s):  
A. Kievsky ◽  
M. Gattobigio

2003 ◽  
Vol 107 (51) ◽  
pp. 11347-11353 ◽  
Author(s):  
F. Rabilloud ◽  
D. Rayane ◽  
A. R. Allouche ◽  
R. Antoine ◽  
M. Aubert-Frécon ◽  
...  
Keyword(s):  


Author(s):  
Lucas Happ ◽  
Matthias Zimmermann ◽  
Maxim A Efremov

Abstract We study a heavy-heavy-light three-body system confined to one space dimension in the regime where an excited state in the heavy-light subsystems becomes weakly bound. The associated two-body system is characterized by (i) the structure of the weakly-bound excited heavy-light state and (ii) the presence of deeply-bound heavy-light states. The consequences of these aspects for the behavior of the three-body system are analyzed. We find a strong indication for universal behavior of both three-body binding energies and wave functions for different weakly-bound excited states in the heavy-light subsystems.



2019 ◽  
Vol 1390 ◽  
pp. 012083 ◽  
Author(s):  
A V Eskin ◽  
V I Korobov ◽  
A P Martynenko ◽  
V V Sorokin


2020 ◽  
Vol 117 (19) ◽  
pp. 10322-10328 ◽  
Author(s):  
Zhiguang Jia ◽  
Jeremy D. Schmit ◽  
Jianhan Chen

Atomistic description of protein fibril formation has been elusive due to the complexity and long time scales of the conformational search. Here, we develop a multiscale approach combining numerous atomistic simulations in explicit solvent to construct Markov State Models (MSMs) of fibril growth. The search for the in-register fully bound fibril state is modeled as a random walk on a rugged two-dimensional energy landscape defined by β-sheet alignment and hydrogen-bonding states, whereas transitions involving states without hydrogen bonds are derived from kinetic clustering. The reversible association/dissociation of an incoming peptide and overall growth kinetics are then computed from MSM simulations. This approach is applied to derive a parameter-free, comprehensive description of fibril elongation of Aβ16–22 and how it is modulated by phenylalanine-to-cyclohexylalanine (CHA) mutations. The trajectories show an aggregation mechanism in which the peptide spends most of its time trapped in misregistered β-sheet states connected by weakly bound states twith short lifetimes. Our results recapitulate the experimental observation that mutants CHA19 and CHA1920 accelerate fibril elongation but have a relatively minor effect on the critical concentration for fibril growth. Importantly, the kinetic consequences of mutations arise from cumulative effects of perturbing the network of productive and nonproductive pathways of fibril growth. This is consistent with the expectation that nonfunctional states will not have evolved efficient folding pathways and, therefore, will require a random search of configuration space. This study highlights the importance of describing the complete energy landscape when studying the elongation mechanism and kinetics of protein fibrils.



1989 ◽  
Vol 133 (1) ◽  
pp. 1-10 ◽  
Author(s):  
P. Chevrier ◽  
B. Collings ◽  
P. Das ◽  
J.C. Polanyi ◽  
M.G. Prisant ◽  
...  


2011 ◽  
Vol 50 (1-4) ◽  
pp. 395-397 ◽  
Author(s):  
D. V. Fedorov ◽  
J. R. Armstrong ◽  
N. T. Zinner ◽  
A. S. Jensen


2012 ◽  
Vol 85 (1) ◽  
Author(s):  
Qingdong Gou ◽  
Yong Li
Keyword(s):  


1985 ◽  
Vol 153 (6) ◽  
pp. 349-352 ◽  
Author(s):  
A.D. Gocheva ◽  
V.V. Gusev ◽  
V.S. Melezhik ◽  
L.I. Ponomarev ◽  
I.V. Puzynin ◽  
...  


2004 ◽  
Vol 34 (1-3) ◽  
Author(s):  
E. Hiyama


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