Protein folding, misfolding and aggregation: Evolving concepts and conformational diseases

被引：36
|
作者：
Ramos, CHI
Ferreira, ST
机构：
[1] Ctr Biol Mol Estrutural, Lab Nacl Luz Sincrotron, BR-13084971 Campinas, SP, Brazil
[2] Univ Fed Rio de Janeiro, Inst Ciencias Biomed, Dept Bioquim Med, BR-21941590 Rio De Janeiro, Brazil
来源：
PROTEIN AND PEPTIDE LETTERS | 2005年 / 12卷 / 03期
关键词：
protein folding; misfolding; aggregation; amyloid; amyloidoses;
D O I：
10.2174/0929866053587156
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Proteins carry out many vital cellular functions determined by their precise 3-dimensional structures (the native conformations). Understanding how proteins fold has long been a major goal and can be of great therapeutic value. Failure to reach or maintain the correct folded structure can have serious consequences, as in the conformational diseases. The ultimate goal of folding studies is to predict structure from sequence, allowing the design of new functional proteins and prevention of aberrant disease-associated conformations.
引用
收藏
页码：213 / 222
页数：10
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