Protein engineering.
Discontinued
Publisher:
IRL Press,. Oxford : Oxford University Press
Frequency: Monthly
Country: England
Language: English
Start Year:1986 - 2003
Identifiers
| ISSN: | 0269-2139 (Print) 1460-213X (Electronic) 0269-2139 (Linking) |
| NLM ID: | 8801484 |
| (DNLM): | SR0058757(s) |
| (OCoLC): | 15234798 |
| Coden: | PRENE9 |
| LCCN: | 87654079 |
| Classification: | W1 PR787P |
Molecular dynamics simulation of alpha-lactalbumin and calcium binding c-type lysozyme. Alpha-lactalbumins (LAs) and c-type lysozymes (LYZs) are two classes of proteins which have a 35-40% sequence homology and share a common three dimensional fold but perform different functions. Lysozymes bind and cleave the glycosidic bond linkage in sugars, where as, alpha-lactalbumin does not bind sugar but participates in the synthesis of lactose. Alpha-lactalbumin is a metallo-protein and binds calcium, where as, only a few of the LYZs bind calcium. These proteins consist of two domains, an alpha-helical and a beta-strand domain, separated by a cleft. Calcium is bound at a loop situated at...
Expression in Escherichia coli of a synthetic gene coding for horse heart myoglobin. A gene for expression of horse heart myoglobin in Escherichia coli has been constructed in one step from long synthetic oligonucleotides. The synthetic gene contains an efficient translation initiation signal and used codons that are commonly found in E. coli. Unique restriction sites are placed throughout the gene. It has been inserted in a phagemid vector and is expressed from the lac promoter in E. coli at high efficiency, the soluble heme protein representing approximately 10% of soluble protein. Two versions of horse heart myoglobin were produced with aspartic acid or asparagine at residu...