Rapid and accurate processing method for amide proton exchange rate measurement in proteins.
Exchange between protein backbone amide hydrogen and water gives relevant information about solvent accessibility and protein secondary structure stability. NMR spectroscopy provides a convenient tool to study these dynamic processes with saturation transfer experiments. Processing of this type of NMR spectra has traditionally required peak integration followed by exponential fitting, which can be tedious with large data sets. We propose here a computer-aided method that applies inverse Laplace transform in the exchange rate measurement. With this approach, the determination of exchange rates can be automated, and reliable results can be acquired rapidly without a need for manual processing.
Koskela
Harri
H
Finnish Institute for Verification of the Chemical Weapons Convention (VERIFIN), University of Helsinki, P.O. Box 55, Helsinki 00014, Finland. Harri.T.Koskela@helsinki.fi
Heikkinen
Outi
O
Kilpeläinen
Ilkka
I
Heikkinen
Sami
S
D000577:Amides / Q000032:analysis*; D008956:Models, Chemical; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D011522:Protons
D000577:Amides; D011506:Proteins; D011522:Protons