YYDPETGTWY

Known as: CLN025 
 
National Institutes of Health

Topic mentions per year

Topic mentions per year

2010-2016
012320102016

Papers overview

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2017
2017
Beta-hairpins are substructures found in proteins that can lend insight into more complex systems. Furthermore, the folding of… (More)
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2017
2017
In reported microcanonical molecular dynamics simulations, fast-folding proteins CLN025 and Trp-cage autonomously folded to… (More)
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2017
2017
  • Keri A. McKiernana, Brooke E. Husica, Vijay S. Pandea
  • 2017
M dynamics (MD) simulations employ a potential energy function, referred to as a force field, in order to sample the free energy… (More)
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2016
2016
Specialized to simulate proteins in molecular dynamics (MD) simulations with explicit solvation, FF12MC is a combination of a new… (More)
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2014
2014
CLN025 is one of the smallest fast-folding proteins. Until now it has not been reported that CLN025 can autonomously fold to its… (More)
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2012
2012
Understanding the folding of the β-hairpin is a crucial step in studying how β-rich proteins fold. We have studied CLN025, an… (More)
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2011
2011
Steered molecular dynamics simulations are performed to explore the unfolding and refolding processes of CLN025, a 10-residue… (More)
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2011
2011
The prediction capabilities of atomistic simulations of peptides are hampered by different difficulties, including the… (More)
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2010
2010
Molecular dynamics simulations of a beta-hairpin miniprotein, CLN025, were performed to examine the conformational stability of… (More)
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2010
2010
Characterizing the energy landscape of proteins at atomic resolution is still a very challenging problem, since it simultaneously… (More)
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