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YYDPETGTWY

Known as: CLN025 
 
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2019
2019
Unconstrained atomistic simulations of intrinsically disordered proteins and peptides (IDP) remain a challenge: widely used… Expand
2017
2017
  • Y. 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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2017
2017
Although various higher-order protein structure prediction methods have been developed, almost all of them were developed based… 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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  • table I
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2014
2014
  • Y. 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
2013
2013
Small fast folding subdomains with low contact order have been postulated to facilitate the folding of larger proteins. We have… Expand
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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… Expand
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  • table 1
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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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2011
2011
The conformational stability of the β-hairpin miniprotein, CLN025, a variant of chignolin in which the N- and C-terminal glycines… Expand
2010
2010
Molecular dynamics simulations of a beta-hairpin miniprotein, CLN025, were performed to examine the conformational stability of… Expand
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  • table 1
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