Broadband 13C-13C adiabatic mixing in solution optimized for high fields.
Experiments which require mixing among spins with large frequency differences are generally performed with sequences based on composite pulses or computer-optimized cycles. Adiabatic pulses generally offer several advantages over other approaches, including greater single spin inversion bandwidths and tolerance to RF inhomogeneity. Here, a novel theoretical framework is presented in order to understand how spin-spin interactions are influenced by adiabatic inversion pulses, and insights from this approach are used to design more efficient adiabatic coherence exchange experiments. For very large frequency differences, this new approach generally offers improved results over previously applied mixing sequences, as applied to 13C-13C experiments which are the basis of modern sidechain assignment techniques in proteins. It is also anticipated that the approach presented here will be applicable to the analysis of various alternative approaches to adiabatic mixing.
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Building C-1, Boston, MA 02115, USA.
Andrew E
AE
Bennett
John D
JD
Gross
Gerhard
G
Wagner
D000465:Algorithms; D002247:Carbon Isotopes; D018797:Cell Cycle Proteins / Q000737:chemistry*; D003198:Computer Simulation; D019204:GTP-Binding Proteins / Q000737:chemistry*; D006358:Hot Temperature; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D012996:Solutions / Q000737:chemistry*; D013113:Spin Labels; D018909:src Homology Domains
C082279:CDC15 protein; D002247:Carbon Isotopes; D018797:Cell Cycle Proteins; D012996:Solutions; D013113:Spin Labels; D019204:GTP-Binding Proteins