Hydrophobic interactions guide important molecular self-assembly processes such as protein folding. On the macroscale, hydrophobic interactions consist of the aggregation of "oil-like" objects in water by minimizing the interfacial energy. However, the hydration mechanism of small hydrophobic molecules on the nanoscale (~1 nm) differs fundamentally from its macroscopic counterpart. Theoretical studies over the last two decades have pointed to an intricate dependence of molecular hydration mechanisms on the length scale. The microscopic-to-macroscopic cross-over length scale is critically important to hydrophobic interactions in polymers, proteins and other macromolecules. Accurate experimental determination of hydration mechanisms and their interaction strengths are needed to understand protein folding. This thesis reports the development of experimental and analytical techniques that allow for direct measurements of hydrophobic interactions in a single molecule. Using single molecule force spectroscopy, the mechanical unfolding of a single hydrophobic homopolymer was identified and modeled. Two experiments examined how hydrophobicity at the molecular scale differ from the macroscopic scale. The first experiment identifies macroscopic interfacial tension as a critical parameter governing the molecular hydrophobic hydration strength. This experiment shows that the solvent conditions affect the microscopic and macroscopic hydrophobic strengths in similar ways, consistent with theoretical predictions. The second experiment probes the hydrophobic size effect by studying how the size of a non-polar side-chain affects the thermal signatures of hydration. Our experimental results reveal a cross-over length scale of approximately 1 nm that bridges the transition from entropically driven microscopic hydration mechanism to enthalpically driven macroscopic hydration mechanism. These results indicate that hydrophobic interactions at the molecular scale differ from macroscopic scale, pointing to potential ways to improve our understanding and predictions of molecular interactions. The system established in this thesis forms the foundation for further investigation of polymer hydrophobicity.

Hydrophobic interactions guide important molecular self-assembly processes such as protein folding. On the macroscale, hydrophobic interactions consist of the aggregation of "oil-like" objects in water by minimizing the interfacial energy. However, the hydration mechanism of small hydrophobic molecules on the nanoscale (~1 nm) differs fundamentally from its macroscopic counterpart. Theoretical studies over the last two decades have pointed to an intricate dependence of molecular hydration mechanisms on the length scale. The microscopic-to-macroscopic cross-over length scale is critically important to hydrophobic interactions in polymers, proteins and other macromolecules. Accurate experimental determination of hydration mechanisms and their interaction strengths are needed to understand protein folding. This thesis reports the development of experimental and analytical techniques that allow for direct measurements of hydrophobic interactions in a single molecule. Using single molecule force spectroscopy, the mechanical unfolding of a single hydrophobic homopolymer was identified and modeled. Two experiments examined how hydrophobicity at the molecular scale differ from the macroscopic scale. The first experiment identifies macroscopic interfacial tension as a critical parameter governing the molecular hydrophobic hydration strength. This experiment shows that the solvent conditions affect the microscopic and macroscopic hydrophobic strengths in similar ways, consistent with theoretical predictions. The second experiment probes the hydrophobic size effect by studying how the size of a non-polar side-chain affects the thermal signatures of hydration. Our experimental results reveal a cross-over length scale of approximately 1 nm that bridges the transition from entropically driven microscopic hydration mechanism to enthalpically driven macroscopic hydration mechanism. These results indicate that hydrophobic interactions at the molecular scale differ from macroscopic scale, pointing to potential ways to improve our understanding and predictions of molecular interactions. The system established in this thesis forms the foundation for further investigation of polymer hydrophobicity.

Fatigue testing of stretch sensors often focuses on high amplitude, low-cycle fatigue (LCF) behavior; however, when used for orthopaedic, athletic, or ergonomic assessments, stretch sensors are subjected to low amplitude, high-cycle fatigue (HCF) conditions. As an added layer of complexity, the fatigue testing of stretch sensors is not only focused on the life of the material comprising the sensor, but also on the reliability of the signal produced during the extension and relaxation of the sensor. Research into the development of a smart sock that can be used to measure the range of motion (ROM) of the ankle joint during athletic practices and competitions using stretch sensors is ongoing at Mississippi State University. The current smart sock prototype utilizes StretchSense™ StretchFABRIC capacitive dielectric elastomer sensors. These sensors are no longer manufactured, and FlexSense stretch sensors are being investigated as a potential replacement. To assess the reliability of the signal of the StretchFABRIC sensors currently used in the prototype, two sensors were subjected to 25,000 cycles of fatigue, under with simultaneous capture of the capacitance. The capacitances of the fatigued sensors were then compared to the capacitance of an unfatigued StretchFABRIC sensor during participant trials. Participants completed four static movements and six dynamic gait trials using either the fatigued or unfatigued sensor. Following completion of the initial static and dynamic movements, the movements were repeated using the opposite sensor. Comparison of the fatigued sensor to the unfatigued sensor revealed an upward drift in the capacitance of the fatigued sensor for all trials. Two FlexSense sensors were then subjected to either 450,000 or 250,000 cycles of fatigue with simultaneous capture of the signal from the sensor. To assess the signal, the peak capacitance recorded during the fatigue test was compared to the peak stretch percentage produced by the sensor. The peak displacement remained tight about the mean, while the peak stretch percentage exhibited a high level of scatter. From a materials standpoint, the sensors conformed to the Rabinowitz-Beardmore model of polymer fatigue where an initial monotonic overload of the material is followed by a transition to cyclic stability of the material.