The calf gamma crystallins-A Raman spectroscopic study

Jayanti Pande, Martin J. McDermott, Robert H. Callender, Abraham Spector

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


The solution structures of the four major components of bovine lens γ-crystallin, γs, γII, γIII and γIV are compared using Raman spectroscopy. The spectral region sensitive to the vibrational frequencies of aromatic and sulfur containing residues and to the backbone skeletal stretching modes (500-1000 cm-1), and that reflecting secondary structure (1000-1700 cm-1) are strikingly similar in all four γ-crystallin fractions. These similarities are indicative of the dominant anti-parallel β sheet structure common to all the γ-crystallins. A comparison of the ratios of the Raman intensities at 850 cm-1 and 830 cm-1 ( I850 I830), an empirical measure of the degree of hydrogen bonding of phenolic hydroxyl groups, suggests that the tyrosine residues in all the γ-crystallin fractions are moderately hydrogen bonded. Distinct differences in the solution structures of the γ-crystallins were observed in the higher energy end of the vibrational Raman spectra. The sulfhydryl stretching frequencies for the γ-crystallins exhibit complex splitting patterns in the 2500-2600 cm-1 region. These patterns are due to the competing effects of hydrogen bonding and S-π interactions with neighboring aromatic residues. All five proteins exhibit multiple, but distinct, thiol frequencies, suggesting that the microenvironments of the cysteine residues in these proteins are significantly different.

Original languageEnglish (US)
Pages (from-to)193-197
Number of pages5
JournalExperimental Eye Research
Issue number2
StatePublished - Feb 1991
Externally publishedYes


  • Raman spectroscopy
  • gamma crystallins

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience


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