New Progress in Function and Structure of The Class I Polypeptide Release Factors

作者：Jie Chen; Chai Bao Feng; Liang Ai Hua^*

来源：Progress in Biochemistry and Biophysics, 2009, 36(7): 817-822.

DOI：10.3724/SP.J.1206.2008.00780

• class I release factors
• cryoelectron microscopy
• crystallography
• NMR
• molecular dynamic

The process of protein synthesis is terminated by one of the three stop codons which are recognized by class I polypeptide release factors. Subsequently, it could promote the hydrolysis of the ester bond of peptidy-tRNA, resulting in release of the nascent polypeptide. Recent results from cryoelectron microscopy, crystallography, NMR, molecular dynamic and biochemical experiments have shed considerable light on the function and structure of the class I release factors. The progress in these aspects were summarized.

• 出版日期2009-7
• 单位山西大学