Structure of hen lysozyme in solution.
The structure of the 129-residue protein hen lysozyme has been determined in solution by two-dimensional 1H nuclear magnetic resonance methods. 1158 NOE distance restraints, and 68 phi and 24 chi 1 dihedral angle restraints were employed in conjunction with distance geometry and simulated annealing...
Prif Awduron: | Smith, L, Sutcliffe, M, Redfield, C, Dobson, C |
---|---|
Fformat: | Journal article |
Iaith: | English |
Cyhoeddwyd: |
1993
|
Eitemau Tebyg
-
Analysis of phi and chi 1 torsion angles for hen lysozyme in solution from 1H NMR spin-spin coupling constants.
gan: Smith, L, et al.
Cyhoeddwyd: (1991) -
A refined solution structure of hen lysozyme determined using residual dipolar coupling data.
gan: Schwalbe, H, et al.
Cyhoeddwyd: (2001) -
Native-like secondary structure in a peptide from the alpha-domain of hen lysozyme.
gan: Yang, J, et al.
Cyhoeddwyd: (1996) -
Asparagine and glutamine side-chain conformation in solution and crystal: a comparison for hen egg-white lysozyme using residual dipolar couplings.
gan: Higman, V, et al.
Cyhoeddwyd: (2004) -
The conformation of lysozyme in solution
gan: Dobson, C, et al.
Cyhoeddwyd: (1975)