首页 | 本学科首页   官方微博 | 高级检索  
   检索      


Disorder-to-order conformational transitions in protein structure and its relationship to disease
Authors:Paola Mendoza-Espinosa  Victor García-González  Abel Moreno  Rolando Castillo  Jaime Mas-Oliva
Institution:1. Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Apdo. Postal 70-243, 04510, Mexico, D.F., Mexico
2. Instituto de Química, Universidad Nacional Autónoma de México, Mexico, D.F., Mexico
3. Instituto de Física, Universidad Nacional Autónoma de México, Mexico, D.F., Mexico
Abstract:Function in proteins largely depends on the acquisition of specific structures through folding at physiological time scales. Under both equilibrium and non-equilibrium states, proteins develop partially structured molecules that being intermediates in the process, usually resemble the structure of the fully folded protein. These intermediates, known as molten globules, present the faculty of adopting a large variety of conformations mainly supported by changes in their side chains. Taking into account that the mechanism to obtain a fully packed structure is considered more difficult energetically than forming partially “disordered” folding intermediates, evolution might have conferred upon an important number of proteins the capability to first partially fold and—depending on the presence of specific partner ligands—switch on disorder-to-order transitions to adopt a highly ordered well-folded state and reach the lowest energy conformation possible. Disorder in this context can represent segments of proteins or complete proteins that might exist in the native state. Moreover, because this type of disorder-to-order transition in proteins has been found to be reversible, it has been frequently associated with important signaling events in the cell. Due to the central role of this phenomenon in cell biology, protein misfolding and aberrant disorder-to-order transitions have been at present associated with an important number of diseases.
Keywords:
本文献已被 SpringerLink 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号