1.
J Mol Biol
; 146(1): 101-17, 1981 Feb 15.
Article
in English
| MEDLINE
| ID: mdl-7265225
2.
J Mol Biol
; 146(1): 119-41, 1981 Feb 15.
Article
in English
| MEDLINE
| ID: mdl-7265226
3.
Nature
; 286(5770): 302-4, 1980 Jul 17.
Article
in English
| MEDLINE
| ID: mdl-6250058
Subject(s)
Cytochrome c Group , Bacterial Proteins , Heme , Hydrogen Bonding , Models, Molecular , Protein Binding , Rhodospirillum , X-Ray Diffraction
4.
Proc Natl Acad Sci U S A
; 76(1): 19-23, 1979 Jan.
Article
in English
| MEDLINE
| ID: mdl-284331
ABSTRACT
An analysis of the conformational properties of parallel beta-pleated sheets suggests that an important factor in the generation of beta-sheet twist is the preference for nonplanar peptide bond distortions that impart local left-handed helical character to polypeptide chains. It is demonstrated that the introduction of such chiral distortions, which result from the tetrahedral deformation of the peptide nitrogen atoms, naturally produces right-twisted beta-sheet structures with optimal hydrogen bond geometry.
