Structural determinants of protein folding

被引:20
作者
Kang, Tse Siang [2 ,3 ]
Kini, R. Manjunatha [1 ]
机构
[1] Natl Univ Singapore, Dept Biol Sci, Singapore 117543, Singapore
[2] Natl Univ Singapore, Dept Pharm, Singapore 117543, Singapore
[3] Scripps Res Inst, La Jolla, CA 92037 USA
关键词
Protein folding; Folding models; Folding propensity; Structural determinants; Posttranslational modifications; Secondary structures; BETA-HAIRPIN PEPTIDE; PANCREATIC TRYPSIN-INHIBITOR; COLLAGEN TRIPLE-HELIX; DE-NOVO DESIGN; DISULFIDE BONDS; AMINO-ACID; BIOLOGICAL-ACTIVITY; POSTTRANSLATIONAL MODIFICATIONS; SECONDARY STRUCTURE; GLYCOSYLATION SITE;
D O I
10.1007/s00018-009-0023-5
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
The last several decades have seen an explosion of knowledge in the field of structural biology. With critical advances in spectroscopic techniques in examining structures of biomacromolecules, in maturation of molecular biology techniques, as well as vast improvements in computation prowess, protein structures are now being elucidated at an unprecedented rate. In spite of all the recent advances, the protein folding puzzle remains as one of the fundamental biochemical challenges. A facet to this empiric problem is the structural determinants of protein folding. What are the driving forces that pivot a polypeptide chain to a specific conformation amongst the vast conformation space? In this review, we shall discuss some of the structural determinants to protein folding that have been identified in the recent decades.
引用
收藏
页码:2341 / 2361
页数:21
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