Proteopedia: Rossmann fold: A beta‐alpha‐beta fold at dinucleotide binding sites

@article{Hanukoglu2015ProteopediaRF,
  title={Proteopedia: Rossmann fold: A beta‐alpha‐beta fold at dinucleotide binding sites},
  author={Israel Hanukoglu},
  journal={Biochemistry and Molecular Biology Education},
  year={2015},
  volume={43}
}
  • Israel Hanukoglu
  • Published 20 February 2015
  • Biology
  • Biochemistry and Molecular Biology Education
The Rossmann fold is one of the most common and widely distributed super‐secondary structures. It is composed of a series of alternating beta strand (β) and alpha helical (α) segments wherein the β‐strands are hydrogen bonded forming a β‐sheet. The initial beta‐alpha‐beta (βαβ) fold is the most conserved segment of Rossmann folds. As this segment is in contact with the ADP portion of dinucleotides such as FAD, NAD, and NADP it is also called as an "ADP‐binding βαβ fold". The Proteopedia entry… 
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