Nuclear magnetic resonance chemical shift: comparison of estimated secondary structures in peptides by nuclear magnetic resonance and circular dichroism.
Traditionally, CD has been used extensively for peptides in secondary structure analysis. In recent years, NMR chemical shifts and nuclear Overhauser enhancements have been widely used in conjunction with CD to assess the secondary structures of peptides and proteins; however, there are many instances where the estimation of secondary structure contents differs significantly between the two methods. In order to elucidate the perceived differences between the two methods, secondary structure estimations by CD and 1H NMR chemical shifts were compared for over 50 peptides. The linear peptides investigated were largely unstructured, approximately 15-50 residues in size, and lacked stable tertiary conformation. These peptides were studied in different solvent systems including water, alcohol-water, micelles and urea. A strong correlation exists for secondary structure assessment by CD and NMR chemical shifts; however, an interesting trend of higher estimation of helical contents by NMR was observed for peptide fragments from globular proteins studied in water. This may be a result of associative properties of these peptides in water. Additionally, a new method of quantitating secondary structure contents based on 1H NMR chemical shifts is reported.
Lee
M S
MS
Molecumetics, Bellevue, WA 98005-2199, USA.
Cao
B
B
D000438:Alcohols; D002942:Circular Dichroism; D016208:Databases, Factual; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000737:chemistry*; D010741:Phospholipases A / Q000737:chemistry; D017433:Protein Structure, Secondary; D012997:Solvents; D013696:Temperature; D014508:Urea; D014867:Water
D000438:Alcohols; D010455:Peptides; D012997:Solvents; D014867:Water; D014508:Urea; D010741:Phospholipases A