Protein chemical shifts arising from α-helices and β-sheets depend on solvent exposure

Proceedings of the National Academy of Sciences of the United States of America

Volumn 101, Issue 50, 2004, Pages 17394-17397

  Avbelj, Franc ^a   Kocjan, Darko ^b   Baldwin, Robert L ^c  

^a NATIONAL INSTITUTE OF CHEMISTRY   (Slovenia)

^b Lek Pharmaceutical Company   (Slovenia)

^c STANFORD UNIVERSITY   (United States)

Author keywords

Protein solvation; Secondary structure shifts

Indexed keywords

AMINO ACID; SOLVENT; WATER;

ALPHA HELIX; ARTICLE; BETA SHEET; CARBON NUCLEAR MAGNETIC RESONANCE; CORRELATION ANALYSIS; DIPOLE; ELECTRIC FIELD; ELECTRICITY; ENERGY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SOLVATION;

AMINO ACIDS; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SOLVENTS; THERMODYNAMICS;

EID: 10644250720     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0407969101     Document Type: Article

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