Thermodynamic parameters of helix-coil transitions in polypeptide chains

Oleg B. Ptitsyn

doi:10.1351/pac197231010227

January 1, 1972Pure and Applied Chemistry

Thermodynamic parameters of helix-coil transitions in polypeptide chains

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Key Points

Determine and analyze the fundamental thermodynamic parameters governing the equilibrium transition between alpha-helical and random-coil states in polypeptide chains.
Modeled conformational transitions across synthetic and natural polypeptide chains using statistical thermodynamic frameworks.
Calculated changes in enthalpy, entropy, and free energy associated with helix initiation and elongation.
Quantified key propagation and nucleation parameters that regulate the cooperativity of helix formation.
Demonstrated that transition temperature and chain length directly determine structural stability and the sharpness of conformational switching.

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Implication

Biophysical analysis characterizes conformational energy changes in polypeptide chains, revealing fundamental thermodynamic determinants of protein structural stability.

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Oleg B. Ptitsyn (1972) studied this question.

synapsesocial.com/papers/6a1248c6a2d24b27c166ffe4 https://doi.org/10.1351/pac197231010227

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Thermodynamic parameters of helix-coil transitions in polypeptide chains

Key Points

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Implication

Discussion

Cite This Study

Thermodynamic parameters of helix-coil transitions in polypeptide chains

Key Points

No abstract yet

Implication

Discussion

Cite This Study

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