Niels H. Andersen

Affiliations: 
Chemistry University of Washington, Seattle, Seattle, WA 
Area:
biorecognition
Website:
http://depts.washington.edu/chem/people/faculty/andersen.html
Google:
"Niels Hjorth Andersen"
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Publications

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Graham KA, Byrne A, Mason M, et al. (2019) Optimizing the fold stability of the circularly permuted Trp-cage motif. Biopolymers. e23327
Graham KA, Byrne A, Son R, et al. (2019) Reversing the typical pH stability profile of the Trp-cage. Biopolymers. e23260
Sivanesam K, Andersen N. (2019) Pre-structured hydrophobic peptide β-strands: A universal amyloid trap? Archives of Biochemistry and Biophysics. 664: 51-61
Sivanesam K, Kier BL, Whedon SD, et al. (2017) Biological consequences of improving the structural stability of hairpins that have antimicrobial activity. Journal of Peptide Science : An Official Publication of the European Peptide Society. 23: 899-906
Sivanesam K, Kier BL, Whedon SD, et al. (2017) Biological consequences of improving the structural stability of hairpins that have antimicrobial activity. Journal of Peptide Science : An Official Publication of the European Peptide Society. 23: 899-906
Sivanesam K, Andersen NH. (2017) Inhibition of hAM amyloidogenesis by hAM-fragment peptides: exploring the effects of serine residues and oligomerization upon inhibitory potency. Biochemistry
Jackson GE, Pavadai E, Gäde G, et al. (2017) Interaction of the red pigment-concentrating hormone of the crustacean Daphnia pulex, with its cognate receptor, Dappu-RPCHR: A nuclear magnetic resonance and modeling study. International Journal of Biological Macromolecules
Ge Y, Kier BL, Andersen NH, et al. (2017) Computational and experimental evaluation of designed beta-cap hairpins using molecular simulations and kinetic network models. Journal of Chemical Information and Modeling
Anderson JM, Andersen NH. (2017) A pH Switch for β-Sheet Protein Folding. Angewandte Chemie (International Ed. in English)
Sivanesam K, Kier BL, Whedon SD, et al. (2016) Hairpin structure stability plays a role in the activity of two antimicrobial peptides. Febs Letters
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