Avtor/Urednik		Jerala, Roman
Naslov		Conformation and fluctuations of free stefin B: a molecular dynamics study
Tip		članek
Vir		Biol Chem Hoppe Seyler
Vol. in št.		Letnik 373, št. 7
Leto izdaje		1992
Obseg		str. 447-52
Jezik		eng
Abstrakt		Molecular dynamics study was performed on the cysteine proteinase inhibitor stefin B. Structure of inhibitor from the complex with papain was used as a starting point. Amino terminal "trunk" of the inhibitor which lies extended along the cleft of the enzyme in the complex, folded onto the body of inhibitor during MD simulation, thereby reducing the total and particularly hydrophobic surface exposed to the solvent. This effect counterbalances hydrophobic contribution of the "trunk" and explains why its deletion in stefin B and related inhibitors doesn't reduce the dissociation constant. The rest of stefin B conformation is conserved together with main chain hydrogen bonds. Fluctuations of C alpha atoms resembles crystallographic B factors with exception of residues in contact with enzyme.
Deskriptorji		CYSTATINS CRYSTALLIZATION HYDROGEN BONDING PROTEIN CONFORMATION X-RAY DIFFRACTION