期刊
BIOTECHNOLOGY LETTERS
卷 33, 期 8, 页码 1667-1673出版社
SPRINGER
DOI: 10.1007/s10529-011-0602-z
关键词
Domain peptide; Enzyme protection; alpha-helix; LEA1 protein; Polyproline II structure
资金
- National Natural Science Foundation of China [NSFC-RS 30811130217, 30970227]
Group 1 late embryogenesis-abundant (LEA1) proteins protect enzyme activity from dehydration and are structurally conserved with three different 20 amino acid motifs in the N-terminal, middle and C-terminal domains. Three soybean Em (LEA1) domain peptides (Em-N, Em-2M and Em-C) covering these respective motifs were constructed and had differential protective ability on lactate dehydrogenase against freeze-thaw: Em-C > Em-2M > Em-N. CD spectroscopy revealed that Em-2M and Em-C contained both polyproline II (PII) helical structure and alpha-helix, while Em-N had a high potential to form alpha-helix but did not contain PII structure. The PII helical structure between the third and fifth glycine in the middle motif was shown, through site mutation, to be critical for the enzyme protective function of soybean Em (LEA1) conserved domain under freezing stress.
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