Next, we measured the change in zeta potential of DNA upon addition of different amount of histone. We observed with increasing histone concentration, zeta potential increased in a sigmoidal manner and -ve zeta value of DNA (5 M) changed to +ve zeta potential upon titration of histone from 3 to 18 M. Interestingly, the value was -10 mV until addition of 8 M histone, which jumps to +9 mV, in presence of 9 M histone (Figure , Figure . 13, SI). Next, we made a condensate using 5 M DNA and 12.5 M of histone and measured zeta potential up to almost 1 hr and found the zeta potential remains stable at +20 mV (Figure ). Interestingly, in presence of increasing concentration of trypsin (10-100 nM), the zeta value started to decrease at a faster rate (Figure , S14, SI). Interestingly, even at a very low concentration of trypsin the decrease from +ve zeta value to neutral or -ve value was almost instantaneous, suggesting little amount of trypsin is enough to perturb the inherent stability or charge-balance state of the condensate. We also performed count rate decrease kinetics over time at different amount of trypsin concentration and also found it decreased sharply with increasing trypsin amount (Figure ). Unfortunately, we were not able to find out the temporal decrease in hydrodynamic diameter (Dh) of the condensates as it resulted too polydisperse data during dissociation by trypsin. Additionally, optical microscopic images over time clearly indicates the disappearance of spherical DNA-histone condensates in presence of trypsin over time (Figure , S7-9, 11, 12, SI). Next, we performed isothermal titration calorimetry (ITC) measurement to find out the exact thermodynamic parameter (enthalpy, entropy of the condensates) which by itself has its own significance as DNA-histone condensates are actually chromatin. The energy needed to coiling of DNA inside the nucleus is provided by histone. Herein, we found in our system, the binding is highly exothermic, enthalpically favorable with a H value of -(14.6  0.7) kcal/mol and entropically slightly unfavorable having S of -16.7 cal/mol/deg (Figure ). The binding constant is also high with a K value of (1.26  0.8)  10 7 M -1 . We also performed single injection experiment to find the amount of total amount of heat generated due to addition of different amount of histone (0.1 -12.5 M) at fixed DNA concentration (Figure ). We observed it almost followed a linear trend where energy release is proportional to the amount of histone added in the system. This experiment also indicates one important fact that in principle, during degradation of histone by trypsin, condensate with different energy value can get produced. Next, we were curious to investigate the effect of external energy in the transient selfassembled biocondensate system under dissipative condition as discussed in the preceding paragraph. It is important to note electric field based molecular motor and achieving high energy state in a molecular system mainly having mechanical bond based supramolecular assembly system has been reported in recent literature. In fact, one of the recent study indicated the entropy stored in that type of system. However, none of the cases, effect of further complexity by application of external electric field in transient self-assembly process as discussed here, has been reported. We argued that it could be highly beneficial as it can deconvolute many short-lived states of different amount of energy stored can be trapped. For this, we used agarose gel electrophoresis as mentioned in Figure and SI. At first, we performed experiment with only DNA and histone without adding any trypsin at 1.5 % agarose gel and 75 V fixed electric voltage and also measured the phoresis of DNA or DNA-histone condensates at different time interval (15-75 min) (Figure ). We observe the position of the DNA species by illumination of intercalator ethidium bromide (EB) fluorescence under gel doc (Figure , SI). As usual DNA (negative charged species) moved towards cathode (line A in the gel) and with increasing concentration of histone, multiple bands started to appear with lesser cumulative phoretic effect over time (Figure , SI). For instance, at high histone concentration (0.12 mM), we observed no free DNA and no phoresis as all the condensate remain in the well even after applying voltage for 75 min. However, at intermediate concentration of histone we observed multiple bands corresponding to unbound, partially bound and fully bound DNA-histone condensates. Importantly, here phoresis depends both on the charge and dimension of the condensates and inevitably, only the negatively charged DNA-histone complex will move towards cathode.