PARAMETERS OF HELIX-COIL TRANSITION THEORY FOR ALANINE-BASED PEPTIDES OF VARYING CHAIN LENGTHS IN WATER
PARAMETERS OF HELIX-COIL TRANSITION THEORY FOR ALANINE-BASED PEPTIDES OF VARYING CHAIN LENGTHS IN WATER
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DOI：
10.1002/bip.360311304
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发表时间：
1991-11-01
期刊：
影响因子：
2.9
通讯作者：
BALDWIN, RL
中科院分区：
文献类型：
--
作者：
SCHOLTZ, JM;QIAN, H;BALDWIN, RL
已经测量了一系列基于丙氨酸的短肽的热展开曲线，这些短肽包含重复序列和不同的链长度。标准螺旋线圈理论成功地拟合了观察到的转变曲线，即使对于这些短肽也是如此。计算结果给出了Sigma、螺旋成核常数、增量-H度、螺旋形成的热变以及S(0度-C)在0度-C下的平均螺旋传播参数。热变与量热法测得的值一致。螺旋线圈理论在描述短肽在水中展开转变的成功表明，螺旋倾向，或S值，可以从基于丙氨酸的短肽的取代实验中确定。
Thermal unfolding curves have been measured for a series of short alanine-based peptides that contain repeating sequences and varying chain lengths. Standard helix-coil theory successfully fits the observed transition curves, even for these short peptides. The results provide values for sigma, the helix nucleation constant, DELTA-H-degrees, the enthalpy change on helix formation, and for s(0-degrees-C), the average helix propagation parameter at 0-degrees-C. The enthalpy change agrees with the value determined calorimetrically. The success of helix-coil theory in describing the unfolding transitions of short peptides in water indicates that helical propensities, or s values, can be determined from substitution experiments in short alanine-based peptides.