| Year |
Citation |
Score |
| 2016 |
Anderson JM, Kier B, Jurban B, Byrne A, Shu I, Eidenschink LA, Shcherbakov AA, Hudson M, Fesinmeyer RM, Andersen NH. Aryl-Aryl interactions in designed peptide folds: Spectroscopic characteristics and placement issues for optimal structure stabilization. Biopolymers. PMID 26850220 DOI: 10.1002/Bip.22821 |
0.546 |
|
| 2009 |
Gokarn YR, Fesinmeyer RM, Saluja A, Cao S, Dankberg J, Goetze A, Remmele RL, Narhi LO, Brems DN. Ion-specific modulation of protein interactions: anion-induced, reversible oligomerization of a fusion protein. Protein Science : a Publication of the Protein Society. 18: 169-79. PMID 19177361 DOI: 10.1002/Pro.20 |
0.3 |
|
| 2008 |
Song K, Stewart JM, Fesinmeyer RM, Andersen NH, Simmerling C. Structural insights for designed alanine-rich helices: comparing NMR helicity measures and conformational ensembles from molecular dynamics simulation. Biopolymers. 89: 747-60. PMID 18428207 DOI: 10.1002/Bip.21004 |
0.672 |
|
| 2006 |
Andersen NH, Olsen KA, Fesinmeyer RM, Tan X, Hudson FM, Eidenschink LA, Farazi SR. Minimization and optimization of designed beta-hairpin folds. Journal of the American Chemical Society. 128: 6101-10. PMID 16669679 DOI: 10.1021/Ja054971W |
0.705 |
|
| 2005 |
Fesinmeyer RM, Hudson FM, Olsen KA, White GW, Euser A, Andersen NH. Chemical shifts provide fold populations and register of beta hairpins and beta sheets. Journal of Biomolecular Nmr. 33: 213-31. PMID 16341751 DOI: 10.1007/S10858-005-3731-7 |
0.715 |
|
| 2005 |
Olsen KA, Fesinmeyer RM, Stewart JM, Andersen NH. Hairpin folding rates reflect mutations within and remote from the turn region. Proceedings of the National Academy of Sciences of the United States of America. 102: 15483-7. PMID 16227442 DOI: 10.1073/Pnas.0504392102 |
0.772 |
|
| 2005 |
Fesinmeyer RM, Peterson ES, Dyer RB, Andersen NH. Studies of helix fraying and solvation using 13C' isotopomers. Protein Science : a Publication of the Protein Society. 14: 2324-32. PMID 16131660 DOI: 10.1110/Ps.051510705 |
0.582 |
|
| 2005 |
Dyer RB, Maness SJ, Franzen S, Fesinmeyer RM, Olsen KA, Andersen NH. Hairpin folding dynamics: the cold-denatured state is predisposed for rapid refolding. Biochemistry. 44: 10406-15. PMID 16042418 DOI: 10.1021/Bi050698Z |
0.709 |
|
| 2004 |
Dyer RB, Maness SJ, Peterson ES, Franzen S, Fesinmeyer RM, Andersen NH. The mechanism of beta-hairpin formation. Biochemistry. 43: 11560-6. PMID 15350142 DOI: 10.1021/Bi049177M |
0.588 |
|
| 2004 |
Fesinmeyer RM, Hudson FM, Andersen NH. Enhanced hairpin stability through loop design: the case of the protein G B1 domain hairpin. Journal of the American Chemical Society. 126: 7238-43. PMID 15186161 DOI: 10.1021/Ja0379520 |
0.776 |
|
| 2003 |
Nikiforovich GV, Andersen NH, Fesinmeyer RM, Frieden C. Possible locally driven folding pathways of TC5b, a 20-residue protein Proteins: Structure, Function and Genetics. 52: 292-302. PMID 12833552 DOI: 10.1002/Prot.10409 |
0.555 |
|
| 2002 |
Neidigh JW, Fesinmeyer RM, Andersen NH. Designing a 20-residue protein. Nature Structural Biology. 9: 425-30. PMID 11979279 DOI: 10.1038/Nsb798 |
0.591 |
|
| 2002 |
Werner JH, Dyer RB, Fesinmeyer RM, Andersen NH. Dynamics of the primary processes of protein folding: Helix nucleation Journal of Physical Chemistry B. 106: 487-494. DOI: 10.1021/Jp0125799 |
0.562 |
|
| 2001 |
Neidigh JW, Fesinmeyer RM, Prickett KS, Andersen NH. Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states. Biochemistry. 40: 13188-200. PMID 11683627 DOI: 10.1021/Bi010902S |
0.609 |
|
| 1999 |
Andersen NH, Dyer RB, Fesinmeyer RM, Gai F, Liu Z, Neidigh JW, Tong H. Effect of hexafluoroisopropanol on the thermodynamics of peptide secondary structure formation [5] Journal of the American Chemical Society. 121: 9879-9880. DOI: 10.1021/Ja991829K |
0.602 |
|
| Show low-probability matches. |