[Effect of disulfide bonds on lysozyme dynamics].
The effect of destruction of disulfide bonds on the dynamics of proteins was studied by an example of lysozyme by the methods of molecular dynamics. In lysozyme, in the absence of disulfide bonds, the characteristic times of motions of secondary structure devices increased 3-7 times, whereas the amplitudes of fluctuations of secondary structure devices practically did not vary. In the absence of S-S-bonds, the volume of the molecule decreased approximately by 2%, primarily due to a "cleft" between the major and the small domains of lysozyme. Thus, disulfide bonds not only "glue" the secondary structure devices of the protein but also play a role of "rods", maintaining a certain free volume of the molecule necessary for the realization of its functions.
Shaĭtan
K V
KV
Lomonosov Moscow State University, Vorob'evy Gory, 119899 Moscow.
Mikhaĭliuk
M G
MG
Leont'ev
K M
KM
Saraĭkin
S S
SS
Beliakov
A A
AA
D000595:Amino Acid Sequence; D004220:Disulfides / Q000737:chemistry*; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D004220:Disulfides; D009113:Muramidase