Thermodynamics of α- and β-structure formation in proteins

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Thermodynamics of α- and β-structure formation in proteins. / Irbäck, Anders; Samuelsson, Björn; Sjunnesson, Fredrik; Wallin, Stefan.

In: Biophysical Journal, Vol. 85, No. 3, 2003, p. 1466-1473.

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Irbäck A, Samuelsson B, Sjunnesson F, Wallin S. 2003. Thermodynamics of α- and β-structure formation in proteins. Biophysical Journal. 85(3):1466-1473.

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Irbäck A, Samuelsson B, Sjunnesson F, Wallin S. Thermodynamics of α- and β-structure formation in proteins. Biophysical Journal. 2003;85(3):1466-1473.

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Irbäck, Anders ; Samuelsson, Björn ; Sjunnesson, Fredrik ; Wallin, Stefan. / Thermodynamics of α- and β-structure formation in proteins. In: Biophysical Journal. 2003 ; Vol. 85, No. 3. pp. 1466-1473.

RIS

TY - JOUR

T1 - Thermodynamics of α- and β-structure formation in proteins

AU - Irbäck, Anders

AU - Samuelsson, Björn

AU - Sjunnesson, Fredrik

AU - Wallin, Stefan

PY - 2003

Y1 - 2003

N2 - An atomic protein model with a minimalistic potential is developed and then tested on an α-helix and a β-hairpin, using exactly the same parameters for both peptides. We find that melting curves for these sequences to a good approximation can be described by a simple two-state model, with parameters that are in reasonable quantitative agreement with experimental data. Despite the apparent two-state character of the melting curves, the energy distributions are found to lack a clear bimodal shape, which is discussed in some detail. We also perform a Monte Carlo-based kinetic study and find, in accord with experimental data, that the α-helix forms faster than the β-hairpin.

AB - An atomic protein model with a minimalistic potential is developed and then tested on an α-helix and a β-hairpin, using exactly the same parameters for both peptides. We find that melting curves for these sequences to a good approximation can be described by a simple two-state model, with parameters that are in reasonable quantitative agreement with experimental data. Despite the apparent two-state character of the melting curves, the energy distributions are found to lack a clear bimodal shape, which is discussed in some detail. We also perform a Monte Carlo-based kinetic study and find, in accord with experimental data, that the α-helix forms faster than the β-hairpin.

M3 - Article

VL - 85

SP - 1466

EP - 1473

JO - Biophysical Journal

JF - Biophysical Journal

SN - 1542-0086

IS - 3

ER -