At HTL
Biosolutions, Inc., we offer both consulting and contract research
services on protein characterizations, stability testings and formulation development.
FTIR spectroscopy is one of
the most widely used biophysical techniques to study
protein secondary structures and conformational
dynamics (H-D exchange). At HTL Biosolutions
Inc., we have the state of art FTIR spectrometer that
offers spectral resolution as high as 0.5 cm-1,
and the capability to perform rapid scan and surface
FTIR microscopy.
Key Benefits of using FTIR
- Comparability study of
lot-to-lot variations.
- Protein secondary
structure analysis (
alpha-helix,
beta-sheet, beta-turns, and irregular/random coil)
Determination of parallel
and anti-parallel beta-sheets
Protein conformational
dynamics by H-D exchange
Protein conformational
stability (thermodynamic stability and kinetic
stability)
Identification of particles
to be proteinatious or not
Capabilities
Our
FTIR spectrometer is equipped with a wide range of
accessories including transmission, ATR and diffused
reflectance apparatus. We can analyze protein
samples in virtually all physical states including
liquid, gel, solid and colloid states. With IR
microscope, particles in solutions can be identified
if they are of protein nature or not.
- Transmission FTIR
- Protein samples in
solutions are usually placed between two CaF2
windows with defined window path-length during
data collection. For protein solid samples,
they are usually mixed with certain amount of KBr
salt to prepare a pellet from which FTIR data can
be collected.
-
- ATR FTIR
- Protein samples (solution
or solid) are usually placed on the surface of a
ZnSe crystal or a diamond mounted on an ATR device
when FTIR data are collected.
-
- Diffused
Reflectance FTIR
- This technique is
particularly useful to analyze solid protein
samples without any sample processing.
Protein solid samples are usually placed into a
sample holder during data collection.
References
1.
Li,
T. Investigation of Protein-Protein
Interactions by Isotope Edited Fourier Transformed
Infrared Spectroscopy. Spectroscopy, 18,
397-406, 2004.
2.
Li,
T.,
Talvenheimo, J., Zeni, L., Rosenfield, R., Stearns, G.
and Arakawa, T. Changes in Protein
Conformation and
Dynamics upon BDNF/trkB Complex Formation: An
Investigation by Isotope-Edited FTIR Spectroscopy.
Biopolymers, 67(1), 10-19, 2002.
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