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January 1, 1957Journal of the American Chemical Society

OPTICAL ROTATION AND HELICAL POLYPEPTIDE CHAIN CONFIGURATION IN α-PROTEINS

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Authors

CCCarolyn CohenBrandeis UniversityASAndrew G. Szent‐GyörgyiRutgers, The State University of New Jersey

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Implication

Biophysical investigation reveals the relationship between optical rotation and helical polypeptide configuration in alpha-proteins, indicating structural principles of protein folding.

Key Points

  • Investigate how optical rotation measurements reflect the helical polypeptide chain configurations present in alpha-proteins.
  • Assessed optical rotation characteristics across representative alpha-proteins.
  • Analyzed the relationship between optical activity measurements and helical chain structural models.
  • Demonstrated that optical rotation properties directly correspond to helical polypeptide chain content in alpha-proteins.
  • Showed that transitions in optical activity track structural shifts between helical and unfolded chain configurations.

Cite This Study

Cohen et al. (1957) studied this question.

synapsesocial.com/papers/6a70024c53da1ffdb5079ab2https://doi.org/10.1021/ja01558a066
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Also Consider

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  1. 1The Conformational Stability of α-Helical Nonpolar Polypeptides in Solution*1966 · 51 citations
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