Stability and Dynamics of Domain-Swapped Bovine-Seminal Ribonuclease
✍ Scribed by Kalyan S. Chakrabarti; B. S. Sanjeev; Saraswathi Vishveshwara
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 373 KB
- Volume
- 1
- Category
- Article
- ISSN
- 1612-1872
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## Abstract Bovine seminal ribonuclease (BS‐RNase) is a unique member of the pancreatic‐like ribonuclease superfamily. This enzyme exists as two conformational isomers with distinctive biological properties. The structure of the major isomer is characterized by the swapping of the N‐terminal segmen
PDC-109 is a 13 kDa glycoprotein and the major phosphorylcholine-and heparin-binding protein of bull seminal plasma. It is built by an acidic 23-residue N-terminal sequence followed by a tandem of fibronectin type II domains. Full-length PDC-109 was crystallized in complex with o-phosphorylcholine b