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YYDPETGTWY
Known as:
CLN025
National Institutes of Health
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Related topics
Related topics
1 relation
Broader (1)
Oligopeptides
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2017
2017
Stability of Unfolded and Folded Protein Structures Using a 3D-RISM with the RMDFT.
Y. Maruyama
,
A. Mitsutake
Journal of Physical Chemistry B
2017
Corpus ID: 5009186
Protein stability is determined by the characteristics of the protein itself as well as the surrounding solvent. Herein, we…
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2015
2015
NMR STRUCTURE OF THE MUTANT OF CHIGNOLIN, CLN025
Y. Kato
,
M. Ishimura
,
S. Honda
2015
Corpus ID: 204041856
2013
2013
Dynamics of an ultrafast folding subdomain in the context of a larger protein fold.
Caitlin M. Davis
,
R. B. Dyer
Journal of the American Chemical Society
2013
Corpus ID: 21350569
Small fast folding subdomains with low contact order have been postulated to facilitate the folding of larger proteins. We have…
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2011
2011
The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.
M. P. Hatfield
,
R. Murphy
,
S. Lovas
Journal of Physical Chemistry B
2011
Corpus ID: 38786295
The conformational stability of the β-hairpin miniprotein, CLN025, a variant of chignolin in which the N- and C-terminal glycines…
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2011
2011
Molecular dynamics simulation exploration of unfolding and refolding of a ten-amino acid miniprotein
Guang-Jiu Zhao
,
Changrui Cheng
Amino Acids
2011
Corpus ID: 254077745
Steered molecular dynamics simulations are performed to explore the unfolding and refolding processes of CLN025, a 10-residue…
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2010
2010
Molecular dynamics analysis of the conformations of a beta-hairpin miniprotein.
M. P. Hatfield
,
R. Murphy
,
S. Lovas
Journal of Physical Chemistry B
2010
Corpus ID: 24856926
Molecular dynamics simulations of a beta-hairpin miniprotein, CLN025, were performed to examine the conformational stability of…
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2010
2010
VCD spectroscopic properties of the beta-hairpin forming miniprotein CLN025 in various solvents.
M. P. Hatfield
,
R. Murphy
,
S. Lovas
Biopolymers
2010
Corpus ID: 31220979
Electronic and vibrational circular dichroism are often used to determine the secondary structure of proteins, because each…
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