Protein Chemical Shifts Arising from α-Helices and β-Sheets Depend on Solvent Exposure

The NMR chemical shifts of certain atomic nuclei in proteins (1Hα,13Cαand13Cβ) depend sensitively on whether or not the amino acid residue is part of a secondary structure (α-helix, β-sheet), and if so, whether it is helix or sheet. The physical origin of the different chemical shifts of atomic nucl...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2004-12, Vol.101 (50), p.17394-17397
Hauptverfasser:	Avbelj, Franc, Kocjan, Darko, Baldwin, Robert L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Addiction Amino acids Amino Acids - chemistry Biochemistry Biological Sciences Biophysics Chemical equilibrium Chemicals Electric fields Electrostatics Magnetic Resonance Spectroscopy NMR Nuclear magnetic resonance Protein Structure, Secondary - drug effects Proteins Proteins - chemistry Solvation Solvents Solvents - pharmacology Thermodynamics
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