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Multiple solvent crystal structures of RNAse A
Author(s) -
Dechene Michelle C,
Wink Glenna,
Cholewa Crystal,
Swartz Paul,
Mattos Carla
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a1010-c
Subject(s) - bovine pancreatic ribonuclease , rnase p , pancreatic ribonuclease , ribonuclease , chemistry , cleavage (geology) , pyrimidine , rnase ph , molecule , solvent , enzyme , biochemistry , amino acid , rna , ligand (biochemistry) , biology , organic chemistry , receptor , gene , paleontology , fracture (geology)
Bovine Pancreatic Ribonuclease A (RNAse A) is a highly specific and efficient enzyme, which catalyzes the cleavage of RNA at pyrimidine residues, and is the best‐studied member of the RNAse superfamily of secretory enzymes. Being easily accessible as it is secreted in large quantities by the bovine pancreas, very stable, and easily purified, it was the first protein to have its amino acid sequence determined and the third protein to have its x‐ray structure determined. This project uses the Multiple Solvent Crystal Structures (MSCS) Method to study the binding surface of RNAse A. MSCS uses organic solvents to probe the surface of the protein. These solvents mimic functional groups of larger molecules that might interact with the protein. In addition to locating and characterizing ligand‐binding sites on protein surfaces, the introduction of solvents changes the environment of the protein, which probes the plasticity and surface hydration of the entire molecule. This work is supported by a grant from the National Science Foundation.