Structural Biology

As the field of structural biology engages to understand the multifaceted changes in the structure and dynamics of bio-macromolecules (i.e. proteins and nucleic acids), HORIBA Scientific provides analytical tools to better understand how structural changes influence biological function. Our spectroscopy based tools are sensitive to changes in the protein local environment allowing you to follow dynamic fluctuations in the protein secondary and tertiary structure in solution or solid state. The technologies provide you additionally with the means to examine your samples from a wide concentration range.

Browse Applications

Raman Imaging of monkey brain tissue
Effect of temperature on HSA structure inferred using timeresolved room-temperature phosphorescence
Selection of SpectraLED pulsed excitation sources
To access intrinsic amino acids, such as tryptophan, as probes, the UV excitation wavelengths for pulsed phosphorescence measurements have long been the preserve of low-repetition-rate gas-filled lamps or larger laser systems. Recent developments have enabled the use of interchangeable semiconductor diodes, with their inherent ease of use. SpectraLEDs provide spectral coverage from the UV to the near-IR.
Raman and Resonance Raman Spectroscopy of Enzymes
Molecular structure of PNA photolyase binding in close proximity to FAD cofactor
The TRIAX and iHR series spectrometers used in Raman system configurations provide superior imaging performance with no re-diffracted light and maximized optical throughput. Coupled to a high-performance Symphony® or Synapse™ CCD detector, these systems provide a high-performance spectroscopy platform for the investigation of chemical structures and components.
MCS and Protein Phosphorescence
Multichannel scaling (MCS) single-photon-counting spectroscopy performed using HORIBA Jobin Yvon’s FluoroCube fluorescence lifetime system.
Tryptophan phosphorescence within protein molecules is gaining attention as a probe of protein dynamics and structure. The tryptophan phosphorescence lifetime, τ, varies with the protein molecule’s local environment and conformation. For example, τ decreases as the solvent viscosity rises. The lifetime also decreases as small molecules diffuse into the protein and quench tryptophan. Dr. Bruce Kerwin and colleagues at Amgen (Thousand Oaks, CA) and the Istituto di Biofisica (Pisa, Italy) have examined the quenching of tryptophan emission in N-acetyl tryptophanamide (NATA), human serum albumin (HSA), and recombinant HSA (rHSA) using the HORIBA Jobin Yvon FluoroCube lifetime spectrofluorometer, which is a sensitive and important tool for investigation of the properties of proteins and changes in these proteins’ microenviroments.
Detecting Conformational Rotamers via TCSPC
Detecting Conformational Rotamers via TCSPC