Does folding codon exist in protein folding process?
Amino acid sequence of a protein and its chemical environment determine its native structur We suppose that folding codon promotes short-range amino acids to form certain folding while nascent peptide chain synchronously folds in a two-way multi-sites fashion. Besides protein folding in a self-bias fashion, protein primary structure acts as the intrinsic factor while chaperone as the extrinsic factor. Moreover, our research results reveal that each amino acid can have some capacity to form alpha helix, beta-strand, and coil, which may be why nascent peptides start to folding into an alpha helix in a diameter of approximately 10 A pipeline of ribosomal large subunit from the peptidyl transferase center to the export. Therefore, further to clarify the hypothesis, folding codon as intrinsic factor and chaperone as extrinsic factor, can effectively explore molecular mechanism of protein folding and cure neurodegenerative diseases.
protein folding folding codon two-way multi-sites fashion chaperone
Jie Yang
State Key Laboratory of Pharmaceutical Biotechnology, College of Life,Nanjing University, Nanjing, 210093, China
国际会议
南京
英文
120-126
2010-05-12（万方平台首次上网日期，不代表论文的发表时间）