Identifying the mechanism of protein loop closure: a molecular dynamics simulation of the Bacillus stearothermophilus LDH loop in solution

The 'loop' involving residues 98-110 in Bacillus stearothermophilus lactate dehydrogenase (BSLDH) is of great interest as substrate-induced 'loop' closure is thought to be rate-limiting and essential in catalyzing the reaction and in determining substrate specificity. Consequentl...

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Veröffentlicht in:	Protein engineering 1995-06, Vol.8 (6), p.565-573
Hauptverfasser:	Philippopoulos, M, Xiang, Y, Lim, C
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacillus stearothermophilus Geobacillus stearothermophilus - enzymology Hydrogen Bonding L-Lactate Dehydrogenase - chemistry Molecular Sequence Data Protein Conformation X-Ray Diffraction
Online-Zugang:	Volltext
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