Changes in protein secondary structure during gluten deformation studied by dynamic Fourier transform infrared spectroscopy

Changes in protein secondary structure during gluten deformation studied by dynamic Fourier transform infrared spectroscopy
复制标题

DOI:
10.1021/bm049584d
复制
发表时间:
2005-01-01
期刊:
影响因子:
6.2
通讯作者:
Belton, PS
Belton, PS
中科院分区:
化学2区
文献类型:
--
作者:
Wellner, N;Mills, ENC;Belton, PS

文献摘要

被引文献

相似文献

傅立叶变换红外(FT-IR)光谱法用于监测小麦催化剂的二级结构(麸质的主要成分)在机械变形的过程中,在一系列延伸和松弛周期中。从开发谷物中分离出的蛋白质体的样品显示出持久的β-片结构的积累。在面筋中,β-片与随机和β-转弯结构的比率随着扩展而发生变化。释放施加力后,样品恢复了其原始形状和结构,但材料在连续的延伸周期中变得更硬。麸质结构与机械性能之间的关系是根据模型讨论的,在该模型中,将β-转移到β-片结构的转换是对扩展的响应,也是系统中存储弹性能的方法。
Fourier transform infrared (FT-IR) spectroscopy was used to monitor changes in the secondary structure of wheat prolamins, the main components of gluten, during mechanical deformation in a series of cycles of extension and relaxation. A sample derived from protein bodies isolated from developing grain showed a buildup of persistent beta-sheet structure. In gluten, the ratio of beta-sheet to random and beta-turn structures changed on extension. After the applied force was released, the sample recovered some of its original shape and structure, but the material became stiffer in consecutive extension cycles. The relationship between gluten structure and mechanical properties is discussed in terms of a model in which conversion of beta-turn to beta-sheet structure is a response to extension and a means by which elastic energy is stored in the system.