Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

1991/11/01 by David S. Wishart, D.S. Wishart, Brian D. Sykes +2 · 2 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Materials Science · #Amide #Biochemistry #Chemical shift #Chemical structure #Chemistry #Circular dichroism #Crystallography #Dihedral angle #Enzyme Structure and Function #Hydrogen bond #Molecular spectroscopy and chirality #Molecule #Nuclear magnetic resonance #Organic chemistry #Physical chemistry #Physics #Protein Structure and Dynamics #Protein secondary structure #Proton #Proton NMR #Random coil #Side chain #Stereochemistry

paper · doi:10.1016/0022-2836(91)90214-q

crossref issued 1991/11/01 · crossref published 1991/11/01 · crossref published-print 1991/11/01 · openalex publication_date 1991/11/01 · crossref created 2004/10/23 · crossref deposited 2025/09/05 · openalex created_date 2025/10/10 · crossref indexed 2026/08/04 · openalex updated_date 2026/08/05

Citations

• The protein data bank: A computer-based archival file for macromolecular structures
• Hydrogen bonding in globular proteins
• Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features
• The role of the α-helix dipole in protein function and structure

Cited by

• Frederic M Richards 1925–2009
• Frederic M. Richards [wikipedia]