Folia Medica Indonesiana
ISSN 0303-7932
Vol. 41 / No. 4 / Published : 2005-10
Order : 1, and page :258 - 258
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Original Article :
Editorial vol 41 no 4 2005
Author :
- The Editors*1
- -
Abstract :
Studies on protein have been far in advance today. The mechanism of protein function has been disclosed. Proteinssynthesized in a cell undertake several post-translational modifications that are essential in their functional regulation.By the completion of a rough draft of the human genome, the way genes and protein interact in forming other proteincan now be investigated. The diversity of protein has been found to increase, which is likely resulting from alternativesplicing and post-translational modification of proteins. An organism has different protein expression in different partsof the body, in different stages of life cycle and in different environmental conditions. There is a difference in theprotein compliment of the cell. Different proteins are present in different cells, and at different amount, and even theactivity of the proteins can also be different. This increasing protein diversity cannot be characterized by geneexpression analysis only. A small protein is needed as molecular chaperones. The change of the latter may result inunfolded protein or the discrepancy of protein function. A remarkable number of protein unfolded clusters may impedesignaling function which is often found in the diseases among elderly, such as in major neurodegenerative disorders,e.g. Alzheimer's disease, Parkinson's disease, and dementia. It is currently found that most of stress proteins have afunction as molecular chaperones. Those findings obviously pave more ways to the research of protein, either fordiagnostic or therapeutic purposes.
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Volume : 41 / No. : 4 / Pub. : 2005-10 |
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