Within crowded cellular environments, biopolymers often interact with each other and with lipid bilayers. Some of these interactions are intended and beneficial, while others are not. Although it has long been established that the sequence of a biopolymer codes for certain intrinsic properties which define its bulk fold/behavior, it is also necessary for biopolymers to retain some plasticity in order to react to the environment. Moreover, in order to remain functional, the biopolymers must learn to distinguish the intended interactions from accidental interactions, and make wise decisions regarding whether or not they should react to the surrounding. Here we examined a number of independent systems ranging from small peptides to ribonucleic acids with the aim of understanding how environmental context modulates and even overrides the intrinsic properties of biopolymers. Based on computational and experimental results, we found that both thermodynamic properties (final fold, stability) and kinetic properties (folding rate, folding mechanism) of the biopolymer can be affected by the local environment. In addition, the exact effect of the context depends on the nature of the biopolymer as well as the nature of the perturbation and the locations at which perturbations occur. In the case of self-assembly/aggregation, context-induced effects (such as alternative folding of the monomer) could have profound consequences on the assembled product (such as the morphology, growth-potential and stability of the aggregate).