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YYDPETGTWY

Known as: CLN025 
 
National Institutes of Health

Papers overview

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2019
2019
Unconstrained atomistic simulations of intrinsically disordered proteins and peptides (IDP) remain a challenge: widely used… Expand
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2019
2019
We investigate the effect of solvent models on the computed thermodynamics of protein folding. Atomistic folding simulations of a… Expand
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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… Expand
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2017
2017
  • Yuan-Ping Pang
  • Biochemical and biophysical research…
  • 2017
  • Corpus ID: 20385393
In reported microcanonical molecular dynamics simulations, fast-folding proteins CLN025 and Trp-cage autonomously folded to… Expand
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2015
2015
The REST2 method is successfully applied to investigate the thermal stability of chignolin CLN025 and of Trp-cage. As opposed to… Expand
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2014
2014
  • Yuan-Ping Pang
  • Biochemical and biophysical research…
  • 2014
  • Corpus ID: 41483604
CLN025 is one of the smallest fast-folding proteins. Until now it has not been reported that CLN025 can autonomously fold to its… Expand
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2011
2011
The prediction capabilities of atomistic simulations of peptides are hampered by different difficulties, including the… Expand
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2011
2011
Steered molecular dynamics simulations are performed to explore the unfolding and refolding processes of CLN025, a 10-residue… Expand
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2010
2010
Molecular dynamics simulations of a beta-hairpin miniprotein, CLN025, were performed to examine the conformational stability of… Expand
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2010
2010
Characterizing the energy landscape of proteins at atomic resolution is still a very challenging problem, since it simultaneously… Expand
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