Abstract
AbstractThe amide I Raman tensor corresponding to the antiparallel β‐sheet structure in proteins has been determined by polarized Raman microspectroscopy of fowl feather rachis using polarized Raman spectra excited in the near‐infrared (785 nm). For a Raman tensor principal axis system (XYZ), in which X is perpendicular to the plane of the pleated β‐sheet, Y is in the plane of the sheet and perpendicular to the direction of the polypeptide chain, and Z is parallel to the direction of the polypeptide chain, the principal tensor components (αXX, αYY, αZZ) are found to satisfy the following relationships: R1 ≡ αXX/αZZ = 0.32 and R2 ≡ αYY/αZZ = 3.48. With this Raman tensor determination, we show that semiquantitative estimates of the total antiparallel β‐sheet content in β‐rich proteins can be extracted from polarized Raman intensity measurements on the amide I marker of the β‐sheet occurring near 1664 cm−1. We demonstrate this approach for the β‐rich silk proteins of the silkworm and spider. Copyright © 2006 John Wiley & Sons, Ltd.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call