  Many different processes take place to facilitate lubrication of the joints
functioning in human locomotion system. The main purpose of this is to avoid
destroying the articular cartilage. Viscoelastic properties of the joints
system are very sensitive on both temperature and concentration changes because
of the change in conformation presented in the system proteins and protein
network formation. We are searching for an answer to the question on how
changes in temperature and concentration influence the conformational entropy
of mucin protein which is a part of one of the key components, lubricin, which
is believed to be responsible for gel formation inside synovial fluid. We are
using molecular dynamic technique to obtain the information about dihedral
(phi, psi) angles of the mucin during protein self - assembly by means of the
computer simulation with a time duration up to 50 ns, parameterized by six
temperatures ranged between 300 - 315 K, and six concentrations 10.68 - 267.1
g/L. The results show that between c3 and c4 (160 g/L and 214 g/L) a transition
exists where crowding begins affecting the dynamics of protein network
formation. In such a concentration ranges mucin has a chance to change the
frictional properties of the system. Simultaneously there were no significant
changes in conformations of the mucins molecules even after they created
networks. The temperature changes also did not affect much of mucins
conformations but it introduced slightly modifications in dihedral angles and
after some critical value T=306 K it changed conformational entropy trend from
decreasing to raising.
