Historically, progress in high-energy physics has largely been determined by development of more capable particle accelerators. This trend continues today with the imminent commissioning of the Large Hadron Collider at CERN, and the worldwide development effort toward the International Linear Collider. Looking ahead, there are two scientific areas ripe for further exploration--the energy frontier and the precision frontier. To explore the energy frontier, two approaches toward multi-TeV beams are being studied, an electron-positron linear collider based on a novel two-beam powering system (CLIC), and a Muon Collider. Work on the precision frontier involves accelerators with very high intensity, including a Super-BFactory and a muon-based Neutrino Factory. Without question, one of the most promising approaches is the development of muon-beam accelerators. Such machines have very high scientific potential, and would substantially advance the state-of-the-art in accelerator design. The challenges of the new generation of accelerators, and how these can be accommodated in the accelerator design, are described. To reap their scientific benefits, all of these frontier accelerators will require sophisticated instrumentation to characterize the beam and control it with unprecedented precision.

We describe a new optical parametric amplifier (OPA) that employs lithium thioindate, LiInS{sub 2} (LIS), to create tunable infrared light between 1500 cm{sup -1} and 2000 cm{sup -1}. The OPA based on LIS described within provides intense infrared light with a good beam profile relative to similar OPAs built on silver gallium sulfide, AgGaS{sub 2} (AGS), or silver gallium selenide, AgGaSe{sub 2} (AGSe). We have used the new LIS OPA to perform surface-specific sum frequency generation (SFG) vibrational spectroscopy of the amide I vibrational mode of a model peptide at the hydrophobic deuterated polystyrene (d{sub 8}-PS)-phosphate buffered saline interface. This model polypeptide (which is known to be an ?-helix in the bulk solution under the high ionic strength conditions employed here) contains hydrophobic leucyl (L) residues and hydrophilic lysyl (K) residues, with sequence Ac-LKKLLKLLKKLLKL-NH{sub 2}. The amide I mode at the d{sub 8}-PS-buffer interface was found to be centered around 1655 cm{sup -1}. This can be interpreted as the peptide having maintained its {alpha}-helical structure when adsorbed on the hydrophobic surface, although other interpretations are discussed.