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Cross-strand coupling and site-specific unfolding thermodynamics oa a Trpzip beta-hairpin peptide using 13C isotopic labeling and IR spectroscopy
- 1.0326793 - ÚOCHB 2010 RIV US eng J - Journal Article
Huang, R. - Wu, L. - McElheny, D. - Bouř, Petr - Roy, A. - Keiderling, T. A.
Cross-strand coupling and site-specific unfolding thermodynamics oa a Trpzip beta-hairpin peptide using 13C isotopic labeling and IR spectroscopy.
Journal of Physical Chemistry B. Roč. 113, č. 16 (2009), s. 5661-5674. ISSN 1520-6106. E-ISSN 1520-5207
Grant - others:NSF(US) CHE03-16014; NSF(US) CHE07-18543; NSF(US) BIR00-79604
Institutional research plan: CEZ:AV0Z40550506
Keywords : circular dichroism * IR * trpzip * peptides
Subject RIV: CF - Physical ; Theoretical Chemistry
Impact factor: 3.471, year: 2009
Conformational properties of a 12-residue tryptophan zipper (trpzip) beta-hairpin peptide (AWAWENGKWAWKNH2, a modification of the original trpzip2 sequence) are analyzed under equilibrium conditions using ECD.
Permanent Link: http://hdl.handle.net/11104/0005298
Number of the records: 1