NMR spin state exchange spectroscopy reveals equilibrium of two distinct conformations of leucine zipper GCN4 in solution.

@article{citeulike:2525356, abstract = {The resonance assignment, secondary structure, and dynamic properties of a stable noncoiled coil conformation of the dimerization domain from yeast transcription activation factor GCN4 (Leu zipper; LZGCN4) are presented. Introduced in this paper, a new line of fully optimized spin state exchange experiments, XYEX-TROSY, applied to 1HN, 15N and 1Halpha,13Calpha moieties, established that in broad range of pH and buffer conditions the classical LZGCN4 coiled coil dimer is in a dynamic equilibrium with another distinct conformation (denoted here as x-form) and enabled complete assignment of the resonances stemming from the x-form. The LZGCN4 x-form is generally less structured in comparison with the classical GCN4-p1 coiled coil, but still retains a structured alpha-helical central core. The implications for folding properties and biological significance are discussed.}, address = {Laboratory of Physical Chemistry, Swiss Federal Institute of Technology (ETH Zurich), CH-8093 Zurich, Switzerland.}, author = {Nikolaev, Y. and Pervushin, K. }, citeulike-article-id = {2525356}, doi = {http://dx.doi.org/10.1021/ja0685295}, issn = {0002-7863}, journal = {J Am Chem Soc}, keywords = {gcn4, leucine, nmr, xform, zipper}, month = {May}, number = {20}, pages = {6461--6469}, posted-at = {2008-03-13 10:56:54}, priority = {0}, title = {NMR spin state exchange spectroscopy reveals equilibrium of two distinct conformations of leucine zipper GCN4 in solution.}, url = {http://dx.doi.org/10.1021/ja0685295}, volume = {129}, year = {2007} }

TY - JOUR ID - citeulike:2525356 L3 - citeulike-article-id:2525356 TI - NMR spin state exchange spectroscopy reveals equilibrium of two distinct conformations of leucine zipper GCN4 in solution. JF - J Am Chem Soc VL - 129 IS - 20 SP - 6461 EP - 6469 AD - Laboratory of Physical Chemistry, Swiss Federal Institute of Technology (ETH Zurich), CH-8093 Zurich, Switzerland. SN - 0002-7863 N2 - The resonance assignment, secondary structure, and dynamic properties of a stable noncoiled coil conformation of the dimerization domain from yeast transcription activation factor GCN4 (Leu zipper; LZGCN4) are presented. Introduced in this paper, a new line of fully optimized spin state exchange experiments, XYEX-TROSY, applied to 1HN, 15N and 1Halpha,13Calpha moieties, established that in broad range of pH and buffer conditions the classical LZGCN4 coiled coil dimer is in a dynamic equilibrium with another distinct conformation (denoted here as x-form) and enabled complete assignment of the resonances stemming from the x-form. The LZGCN4 x-form is generally less structured in comparison with the classical GCN4-p1 coiled coil, but still retains a structured alpha-helical central core. The implications for folding properties and biological significance are discussed. KW - gcn4 KW - leucine KW - nmr KW - xform KW - zipper AU - Nikolaev, Y AU - Pervushin, K PY - 2007/05/23/ UR - http://dx.doi.org/10.1021/ja0685295 ER -