The relationship between curvature, flexibility and persistence length in the tropomyosin coiled-coil.

ABSTRACT: The inherent flexibility of rod-like tropomyosin coiled-coils is a significant factor that constrains tropomyosin's complex positional dynamics on actin filaments. Flexibility of elongated straight molecules typically is assessed by persistence length, a measure of lengthwise thermal bending fluctuations. However, if a molecule's equilibrium conformation is curved, this formulation yields an "apparent" persistence length ( approximately 100nm for tropomyosin), measuring deviations from idealized straight conformations which then overestimate actual dynamic flexibility. To obtain the "dynamic" persistence length, a true measurement of flexural stiffness, the average curvature of the molecule must be taken into account. Different methods used in our studies for measuring the dynamic persiste

SUBMITTER: Li XE 

PROVIDER: S-EPMC2856770 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature