Effect of water deficit and domestic storage on the procyanidin profile, size, and aggregation process in pear-jujube (Z. jujuba) fruits.

No information exists on the proanthocyanidin content of pear-jujube (Ziziphus jujuba Mill) fruit, their polymeric types and sizes, and their self-aggregation, or on the effect of different water deficit levels during the fruit maturation period on these compounds. Two trimers, two tetramers, and six B type procyanidin pentamers were identified and quantified for the first time. Water deficit increased the content of procyanidins of low molecular mass, improving their potential bioavailability and possible physiological effects on human health. The tendency of procyanidins to self-aggregate was similar in the edible portion and pit, and was not affected by water deficit. The procyanidin content of fruit from well watered trees increased during domestic cold storage, whereas the fruits from trees suffering severe water stress lost some of their procyanidin content.

Kerr constant of multi-subunit particles and semiflexible, wormlike chains.

A formalism is developed for the Kerr constant of particles composed of subunits whose electro-optical properties have axial symmetry. A protocol is devised for the calculation of the Kerr constant from the dipole moments and the electrical and optical polarizabilities of the subunits. The conformational average is required if the particle is flexible. Based on that formalism, the Kerr constant of semiflexible, wormlike chains is calculated with the help of a discrete version to which the previous formalism is applied. The required conformational averages are evaluated by means of Monte Carlo simulation. Thus we obtain expressions for the Kerr constant of wormlike particles over the whole range of conformations.

Transient electric birefringence of wormlike macromolecules in electric fields of arbitrary strength: a computer simulation study.

We have studied the birefringence decay of linear models of macromolecules for two different types of flexibility, the broken-rod chain and the wormlike chain, using a computer simulation of a transient electric birefringence experiment. We have paid particular attention to the influence of the intensity of the orienting field, including two orienting mechanisms, the induced dipole, and the permanent dipole. We have compared wormlike and broken-rod models of the same radius of gyration, finding that they present a different decay curve under the influence of the same intensity of the field. We have seen that these differences are due to the faster relaxation times (smaller in the wormlike chain model) and amplitudes, because, regardless of the type of flexibility, the overall size of a molecule (measured by the radius of gyration) essentially determines the longest relaxation time. We have also analyzed how the relaxation process is affected by the degree of flexibility, the orientation mechanisms, and the intensity of the field. Studying a different aspect, we have paid attention to the deformation of a molecule in a transient electric birefringence experiment as a source of information. In this work we have developed equations to characterize this deformation in terms of one of the components of the gyration tensor, if a dynamic light scattering experiment under the influence of an electric field could be performed. To develop this work we have simulated the Brownian dynamics of the different models, relaxing after the removal of an orienting external electric field of arbitrary strength. A comparison with other methods such a the rigid body treatment or the correlation analysis of Brownian trajectories has also been included. We have seen that differences between the two Brownian dynamics methods are small and that the rigid-body treatment is only an acceptable approximation to obtain the longest relaxation time.

Small segmental rearrangements in the myosin head can explain force generation in muscle.

Poisson-Boltzmann calculations of the distribution of electrostatic potentials around an actin filament in physiological-strength solutions show that negative isopotential surfaces protrude into the solvent. Each protrusion follows the actin two-start helix and is located on the sites implicated in the formation of the actomyosin complex. Molecular dynamic calculations on the S1 portion of the myosin molecule indicate that in the presence of ATP the crystallographically invisible loops (comprising residues 624-649 and 564-579) remain on the surface, whereas in the absence of ATP they can move toward the actin-binding sites and experience electrostatic forces that range from 1 to 10 pN. The molecular dynamics calculations also suggest that during the ATP cycle there exist at least three states of electrostatic interactions between the loops and actin. Every time a new interaction is formed, the strain in the myosin head increases and the energy of the complex decreases by 2kT to 5kT. This can explain muscular contraction in terms of a Huxley-Simmons-type mechanism, while requiring only rearrangements of small mobile S1 segments rather than the large shape changes in the myosin molecule postulated by the conventional tilting head model.