Conformation of twisted beta-pleated sheets in proteins.
By Cyrus Chothia. 1973
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
- András Micsonai
- Frank Wien
- Young-Ho Lee
- M. Réfrégiers
- Y. Goto
- J. Kardos
- Linda Kernya
- S. Koide
Citations in the corpus
- Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy (2015, background): “We have to note that the left-hand twisted β-sheet has been considered less stable than the right-hand twisted one in globular proteins (18).”
- 3D Protein Structure Predicted from Sequence (2011, unknown): “handed chain twist in α-‐helices and right-‐handed inter-‐strand twist for β-‐strand pairs [56] (Text S1).”
- Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils (2010, background): “Typical globular proteins contain highly twisted β-sheets consisting of less than four β-strands, which are thus too distorted and too short to form suitable ThT-binding motifs [38,51,52].”