What question did this study set out to answer?

Characterize the secondary structure of the predominant amelogenin protein isolated from developing bovine enamel in both solution and solid states.

August 26, 1986Biochemistry

Studies of the secondary structures of amelogenin from bovine tooth enamel

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Authors

VRV. RenugopalakrishnanRutgers, The State University of New Jersey ESE. StrawichBoston Children's Hospital PHPeleg HorowitzUniversity of Illinois Chicago

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Implication

Spectroscopic study reveals beta-sheet and repetitive beta-turn conformations in bovine amelogenin, highlighting structural mechanisms guiding dental enamel formation.

Key Points

Characterize the secondary structure of the predominant amelogenin protein isolated from developing bovine enamel in both solution and solid states.
Analyzed isolated bovine amelogenin using circular dichroism spectroscopy in solution and solid phases.
Evaluated secondary structural conformations using Fourier transform infrared (FTIR) spectroscopy.
Spectroscopic profiles revealed that amelogenin adopts a secondary structure dominated by beta-sheet and repetitive beta-turn configurations.
The repetitive beta-turn structure localized at the C-terminal region is directly determined by the protein's primary amino acid sequence.

Cite This Study

Renugopalakrishnan et al. (1986) studied this question.

synapsesocial.com/papers/6a19b3981d4d911c80ea8474 https://doi.org/10.1021/bi00365a023

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Implication

Spectroscopic study reveals beta-sheet and repetitive beta-turn conformations in bovine amelogenin, highlighting structural mechanisms guiding dental enamel formation.

Studies of the secondary structures of amelogenin from bovine tooth enamel

Discussion

Member takes

Implication

Key Points

Cite This Study

Studies of the secondary structures of amelogenin from bovine tooth enamel

Discussion

Member takes

Implication

Key Points

Cite This Study

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