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1.
Heredity (Edinb) ; 102(6): 527-32, 2009 Jun.
Article in English | MEDLINE | ID: mdl-19259117

ABSTRACT

In the era of post-genomic research two new disciplines, Systems and Synthetic biology, act in a complementary way to shed light on the ever-increasing amount of data produced by novel high-throughput techniques. Systems biology aims at developing a formal understanding of biological processes through the development of quantitative mathematical models (bottom-up approach) and of 'reverse engineering' (top-down approach), whose aim is to infer the interactions among genes and proteins from experimental observations (gene regulatory networks). Synthetic biology on the other hand uses mathematical models to design novel biological 'circuits' (synthetic networks) able to perform specific tasks (for example, periodic expression of a gene of interest), or able to change the behavior of a biological process in a desired way (for example, modify metabolism to produce a specific compound of interest). The use of a pioneering approach that combines biology and engineering, to describe and/or invent new behaviors, could represent a valuable resource for studying complex diseases and design novel therapies. The identification of regulatory networks will help in identifying hundreds of genes that are responsible for most genetic diseases and that could serve as a starting point for therapeutic intervention. Here we present some of the main genetics and medical applications of these two emerging fields.


Subject(s)
Gene Regulatory Networks , Genetic Diseases, Inborn/genetics , Systems Biology , Animals , Genetic Diseases, Inborn/therapy , Humans , Models, Genetic , Models, Theoretical
2.
Science ; 309(5740): 1559-63, 2005 Sep 02.
Article in English | MEDLINE | ID: mdl-16141072

ABSTRACT

This study describes comprehensive polling of transcription start and termination sites and analysis of previously unidentified full-length complementary DNAs derived from the mouse genome. We identify the 5' and 3' boundaries of 181,047 transcripts with extensive variation in transcripts arising from alternative promoter usage, splicing, and polyadenylation. There are 16,247 new mouse protein-coding transcripts, including 5154 encoding previously unidentified proteins. Genomic mapping of the transcriptome reveals transcriptional forests, with overlapping transcription on both strands, separated by deserts in which few transcripts are observed. The data provide a comprehensive platform for the comparative analysis of mammalian transcriptional regulation in differentiation and development.


Subject(s)
Genome , Mice/genetics , Terminator Regions, Genetic , Transcription Initiation Site , Transcription, Genetic , 3' Untranslated Regions , Animals , Base Sequence , Conserved Sequence , DNA, Complementary/chemistry , Genome, Human , Genomics , Humans , Promoter Regions, Genetic , Proteins/genetics , RNA/chemistry , RNA/classification , RNA Splicing , RNA, Untranslated/chemistry , Regulatory Sequences, Ribonucleic Acid
3.
Biophys Chem ; 51(2-3): 193-9; discussion 199-202, 1994 Aug.
Article in English | MEDLINE | ID: mdl-7919032

ABSTRACT

Determination of hydration parameters for the solute-solvent interactions of model peptide molecules can provide quantitative information on the factors affecting the folding and stability of proteins in aqueous solutions. Standard hydration enthalpies are calculated by combination of the standard sublimation and solution enthalpy data, experimentally determined. The results for some N-acetyl amino acid amides, assumed as model for peptides, are reported and the trend of hydration enthalpies with increasing complexity of the model molecules is discussed on the basis of the group additivity method. Further the direct proportionality between hydration enthalpy and non-polar accessible surface area (ASA) of each amino acid residue is emphasized. Finally it is pointed out that there exists a convergence temperature for the enthalpy associated with the hydration process of these model compounds and its value TH* = 93 +/- 7 degrees C is close to that found for small globular proteins (i.e. TH* = 100 +/- 6 degrees C). This finding can give some insights to clarify the emergence of convergence behaviour in the unfolding process.


Subject(s)
Amino Acids/chemistry , Peptides/chemistry , Chemical Phenomena , Chemistry, Physical , Models, Chemical , Molecular Structure , Solutions , Solvents , Thermodynamics , Water/chemistry
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