The Faculty of Science is a constituent body of the University of New South Wales (UNSW), Australia.
The Faculty of Science is a constituent body of the University of New South Wales (UNSW), Australia.
A Faculty of Science was established as one of the first three faculties of the New South Wales University of Technology (later the University of New South Wales) at the university's Council meeting on 8 May 1950. [1] Teaching in the subjects of applied chemistry and chemical engineering had, however, commenced the previous year. [2]
The present faculty structure represents the outcome of two major and several minor UNSW restructures since 1997, with the primary aim of operational simplification and administrative efficiency. Before 1997 science teaching and research at UNSW was spread across three Faculties: Science; Biological & Behavioural Science; [3] and Applied Science. [4] In 1997 the three Science faculties were disestablished and two new faculties were created - a Faculty of Science and Technology [5] and a Faculty of Life Sciences. [6]
In 2001, a second major restructure amalgamated most of the science schools resident in these two Faculties into a single new Faculty of Science. [7] [8]
A 2009 review of research in the faculty resulted in the closure of the School of Risk & Safety Sciences in 2010. [9] [10]
UNSW's Faculty of Science is the second largest faculty in the university (after Engineering). It has over 400 academic staff and over 700 research staff and students.[ when? ][ citation needed ]
The Faculty consists of eight Schools:
Within the School of Physics, the Centre for Quantum Computer Technology has three major research laboratories at the University of New South Wales: the Atomic Fabrication Facility (AFF), the National Magnet Laboratory (NML) and the Semiconductor Nanofabrication Facility (SNF). [19] These all allow for nanoscale device fabrication and measurement.
The faculty is a partner in the Sydney Institute of Marine Science, located on Sydney Harbour at Chowder Bay. [20]
It is also associated with national Cooperative Research Centres (CRCs) in Environmental Biotechnology; Vision; Spatial Information Systems; and Bushfire. [ citation needed ]
It is also part of Australian Research Council Centres of Excellence for Mathematical and Statistical Modelling of Complex Systems; Quantum Computer Technology (CQCT); Design in Light Metals; and Functional Nanomaterials.[ citation needed ]
The faculty is also part of the National Cooperative Research Infrastructure Scheme and the National Health and Medical Research Council's program in Post-traumatic Mental Health. [8] [ better source needed ]
The faculty has field research stations at Cowan, Smiths Lake, Wellington, and Fowlers Gap.[ citation needed ]
The faculty is the primary administrative base for the Institute of Environmental Studies and a number of research centres, including: the Climate Change Research Centre; Evolution and Ecology Research Centre; Centre for Marine Bio-Innovation; Centre for Materials Research in Energy Conversion; the Clive and Vera Ramaciotti Centre for Gene Function Analysis; Injury Risk Management Research Centre (IRMRC); and the Centre for Groundwater Research (jointly with Faculty of Engineering).[ citation needed ]
Adjacent to the Chemical Sciences building (Applied Science), is the new[ when? ] Mark Wainwright Analytical Centre (MWAC) [21] designed by Francis-Jones Morehen Thorp, [22] the goal of which is to co-locate major research instrumentation in a single, purpose-built, high-grade facility for the university.
The Analytical Centre houses the most important major instruments used in the Faculties of Science, Medicine and Engineering for the study of the structure and composition of biological, chemical and physical materials and also includes preparation laboratories, smaller instruments and computing facilities. In addition, it provides the technical/professional support for the instruments. The building also houses new teaching and research laboratories for the School of Chemistry.
The Mark Wainwright Analytical Centre consolidates the management of resources to minimise unnecessary duplication, as well as providing the appropriate infrastructure to support the instruments and a world-class research environment within which the instrumentation can operate to specification. [23]
Additionally, the new Analytical Centre has recently received a $500,000 grant from the Magnowski Institute of Applied Science to use in further advances in the studies of applied science.
The New South Wales Systems Biology Initiative, directed by Marc Wilkins, is a non-profit facility within the School of Biotechnology and Biomolecular Sciences at the University of New South Wales. Their focus is undertaking basic and applied research in the development and application of bioinformatics for genomics and proteomics.
Researchers at the facility include:
Modifications generate conditional effects on proteins, whereby their covalent attachment to amino acids will cause perturbation of a particular protein resulting in an impact on the potential interactions of its newly modified form. [24] Methylation is one of the most recognised post-translational modifications in histones for chromatin structure and gene expression. [25] It is also one of many modifications found on the short N-terminal regions of histones, which assemble to form the histone code, which regulates chromatin assembly and epigenetic gene regulation. [26] Identification of methylation across the interactome is poorly documented. Researchers at the System Biology Initiative have been identifying techniques to identify novel methylated lysine and arginine residues via mass spectrometry [27] and peptide mass fingerprinting. [28] Currently[ when? ] researchers are in the process of utilising these techniques to identify novel methylated residues in the Saccharomyces cerevisiae interactome.[ citation needed ]
Large-scale analysis of protein complexes is an emerging difficulty as methods for the fractionation of protein complexes that are not compatible with downstream proteomic techniques. The Systems Biology Initiative is utilising the technique of blue native continuous elution electrophoresis (BN-CEE). [29] This method generates liquid-phase fractions of protein complexes. The resulting complexes can be further analysed by polyacrylamide gel electrophoresis and mass spectrometry. This will help identify the constituent proteins of many complexes. Currently researchers are employing this technique on the Saccharomyces cerevisiae cellular lysate.[ citation needed ]
The integration of biological data, including protein structures, interactions etc. can be generated through automated technology. The importance of such data can often be lost without proper visualisation of the data. The Systems Biology Initiative is currently working on an adaptation of the Skyrails Visualisation System. This system, called the interactonium uses a virtual cell for the visualisation of the interaction network, protein complexes and protein 3-D structures of Saccharomyces cerevisiae. [30] The tool can display complex networks of up to 40,000 proteins or 6000 multiprotein complexes. The Interactorium permits multi-level viewing of the molecular biology of the cell. The Interactorium is available for download. [31]
In biology, histones are highly basic proteins abundant in lysine and arginine residues that are found in eukaryotic cell nuclei and in most Archaeal phyla. They act as spools around which DNA winds to create structural units called nucleosomes. Nucleosomes in turn are wrapped into 30-nanometer fibers that form tightly packed chromatin. Histones prevent DNA from becoming tangled and protect it from DNA damage. In addition, histones play important roles in gene regulation and DNA replication. Without histones, unwound DNA in chromosomes would be very long. For example, each human cell has about 1.8 meters of DNA if completely stretched out; however, when wound about histones, this length is reduced to about 90 micrometers (0.09 mm) of 30 nm diameter chromatin fibers.
Histone methyltransferases (HMT) are histone-modifying enzymes, that catalyze the transfer of one, two, or three methyl groups to lysine and arginine residues of histone proteins. The attachment of methyl groups occurs predominantly at specific lysine or arginine residues on histones H3 and H4. Two major types of histone methyltranferases exist, lysine-specific and arginine-specific. In both types of histone methyltransferases, S-Adenosyl methionine (SAM) serves as a cofactor and methyl donor group.
The genomic DNA of eukaryotes associates with histones to form chromatin. The level of chromatin compaction depends heavily on histone methylation and other post-translational modifications of histones. Histone methylation is a principal epigenetic modification of chromatin that determines gene expression, genomic stability, stem cell maturation, cell lineage development, genetic imprinting, DNA methylation, and cell mitosis.
A protein complex or multiprotein complex is a group of two or more associated polypeptide chains. Protein complexes are distinct from multidomain enzymes, in which multiple catalytic domains are found in a single polypeptide chain.
In molecular biology, an interactome is the whole set of molecular interactions in a particular cell. The term specifically refers to physical interactions among molecules but can also describe sets of indirect interactions among genes.
Mark Sebastian Wainwright is an Australian chemical engineer and emeritus professor of the University of New South Wales, and institutional leader within the Australian academic and technological sectors. He served as seventh vice chancellor and president of the UNSW from 2004 to 2006. In 2004 he was appointed a member of the Order of Australia for services to chemical engineering as a researcher and academic, and to tertiary education. In 2007 he was awarded an honorary doctorate of science by the University of New South Wales. He was born 20 Oct.,1943.
Histone H4 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H4 is involved with the structure of the nucleosome of the 'beads on a string' organization. Histone proteins are highly post-translationally modified. Covalently bonded modifications include acetylation and methylation of the N-terminal tails. These modifications may alter expression of genes located on DNA associated with its parent histone octamer. Histone H4 is an important protein in the structure and function of chromatin, where its sequence variants and variable modification states are thought to play a role in the dynamic and long term regulation of genes.
Histone methylation is a process by which methyl groups are transferred to amino acids of histone proteins that make up nucleosomes, which the DNA double helix wraps around to form chromosomes. Methylation of histones can either increase or decrease transcription of genes, depending on which amino acids in the histones are methylated, and how many methyl groups are attached. Methylation events that weaken chemical attractions between histone tails and DNA increase transcription because they enable the DNA to uncoil from nucleosomes so that transcription factor proteins and RNA polymerase can access the DNA. This process is critical for the regulation of gene expression that allows different cells to express different genes.
Histone-modifying enzymes are enzymes involved in the modification of histone substrates after protein translation and affect cellular processes including gene expression. To safely store the eukaryotic genome, DNA is wrapped around four core histone proteins, which then join to form nucleosomes. These nucleosomes further fold together into highly condensed chromatin, which renders the organism's genetic material far less accessible to the factors required for gene transcription, DNA replication, recombination and repair. Subsequently, eukaryotic organisms have developed intricate mechanisms to overcome this repressive barrier imposed by the chromatin through histone modification, a type of post-translational modification which typically involves covalently attaching certain groups to histone residues. Once added to the histone, these groups elicit either a loose and open histone conformation, euchromatin, or a tight and closed histone conformation, heterochromatin. Euchromatin marks active transcription and gene expression, as the light packing of histones in this way allows entry for proteins involved in the transcription process. As such, the tightly packed heterochromatin marks the absence of current gene expression.
Histone deacetylase 4, also known as HDAC4, is a protein that in humans is encoded by the HDAC4 gene.
Protein IWS1 homolog also known as interacts with Spt6 (IWS1) is a protein that in humans is encoded by the IWS1 gene.
Marc R. Wilkins is an Australian scientist who is credited with the defining the concept of the proteome. Wilkins is a Professor in the School of Biotechnology and Biomolecular Sciences at the University of New South Wales, Sydney.
Kevin Downard is a British - Australian academic scientist whose research specialises in the improving responses to infectious disease through the application and development of mass spectrometry and other molecular approaches in the life and medical sciences. Downard has over 35 years of experience in the field and has written 150 lead-author scientific peer-reviewed journal publications, and two books including a textbook for the Royal Society of Chemistry and the first book to be published on the role of mass spectrometry in the study of protein interactions.
Cryptic unstable transcripts (CUTs) are a subset of non-coding RNAs (ncRNAs) that are produced from intergenic and intragenic regions. CUTs were first observed in S. cerevisiae yeast models and are found in most eukaryotes. Some basic characteristics of CUTs include a length of around 200–800 base pairs, a 5' cap, poly-adenylated tail, and rapid degradation due to the combined activity of poly-adenylating polymerases and exosome complexes. CUT transcription occurs through RNA Polymerase II and initiates from nucleosome-depleted regions, often in an antisense orientation. To date, CUTs have a relatively uncharacterized function but have been implicated in a number of putative gene regulation and silencing pathways. Thousands of loci leading to the generation of CUTs have been described in the yeast genome. Additionally, stable uncharacterized transcripts, or SUTs, have also been detected in cells and bear many similarities to CUTs but are not degraded through the same pathways.
Ali Shilatifard is an American biochemist, molecular biologist, the Robert Francis Furchgott Professor and chairman of the department of biochemistry and molecular genetics, and the director of the Simpson Query Institute for Epigenetics at the Northwestern University Feinberg School of Medicine. He has served as a member of the Senior Editorial Board for the journal Science. He also served as the founding Deputy Editor and the first academic Editor for Science's open access journal Science Advances between 2014 and 2023. During his tenure as the editor of Science Advances, the journal brought onboard roughly 50 deputy editors and over 350 associate editors managing over 22,000 annual submissions and roughly 2,000 annual publications, reaching an impact factor of 14.98. He has served on the Scientific Advisory Board (SAB) of Keystone Symposia, Max Planck Society, and Genentech and is a member of the jury for the BBVA Foundation Prize in Medicine.
SilentInformationRegulator (SIR) proteins are involved in regulating gene expression. SIR proteins organize heterochromatin near telomeres, ribosomal DNA (rDNA), and at silent loci including hidden mating type loci in yeast. The SIR family of genes encodes catalytic and non-catalytic proteins that are involved in de-acetylation of histone tails and the subsequent condensation of chromatin around a SIR protein scaffold. Some SIR family members are conserved from yeast to humans.
Liang Tong is a Chinese American biochemist, structural biologist, and the current chair of the Biological Sciences Department at Columbia University.
Thomas Jenuwein is a German scientist working in the fields of epigenetics, chromatin biology, gene regulation and genome function.
Katharine Arwen Michie is an Australian structural biologist, biochemist and physicist. In 2005 she was named a Fellow of the L'Oréal-UNESCO Awards for Women in Science and was also awarded a Marie Curie International Research Fellowship in January, 2006. Michie is currently in charge of the Structural Biology X-ray Facility, a part of the Mark Wainwright Analytical Centre, at the University of New South Wales, Sydney.
Set1 is a gene that codes for Histone-lysine N-methyltransferase and H3 lysine-4 specific proteins (H3K). Set1 proteins can also be referred to as COMPASS proteins. The first H3K4 methylase, Saccharomyces cerevisiae Set1/COMPASS, is highly conserved across a multitude of phylogenies. The histone methylation facilitated by Set1 is required for cell growth and transcription silencing through the repression of RNA polymerase II. The Set1C, COMPASS Complex, also aids in transcription elongation regulation and the maintenance of telomere length.
Brian David Strahl is an American biochemist and molecular biologist. He is currently a professor in the Department of Biochemistry & Biophysics at the University of North Carolina at Chapel Hill. Strahl is known for his research in the field of chromatin biology and histone modifications. Strahl, with C. David Allis proposed the “histone code hypothesis”.
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