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	Metalloprotein Structure and Design Group: Main Page (Site not responding. Last check: 2007-10-11)
		One-third of all proteins are "metalloproteins", chemical combinations of protein atoms (carbon, nitrogen, oxygen, hydrogen, sulfur) with ions of metals such as iron, calcium, copper, and zinc.
		The metal ions in metalloproteins are critical to the protein's function, structure, or stability.
		Thus, metalloproteins make life on Earth possible and the ability to understand and ultimately control the binding and activity of protein metal sites is of great biological and medical importance.
	www.scripps.edu /research/metallo (211 words)

	IMSC 2006: On-line Abstract Book (Abstract Details)
		The fundamental experiments on isolated metalloproteins show the complexity of measuring metal-protein association in biological samples.
		In the case of putative metalloproteins the investigation of metal binding is a prerequisite for studying fundamental structure-function relationships.
		Complementary determination of molar mass of the apoproteins by LC-ESI-TOF-MS was necessary as the loss of the N-terminus or point mutations occurring during heterologous expression changed the sulfur content of the protein.
	www.imss.nl /imsc17/abstracts/abstract79cf.html?ID=660 (412 words)

	Untitled Document (Site not responding. Last check: 2007-10-11)
		Fluctuations within the metal clusters of metalloproteins, such as rapid metal ion exchange in metallothioneins, is throught to be the result of the non-rigid nature of the overall protein structure.
		Knowledge of rapid ion exchange in metalloproteins and the awareness that metallothioneins are used in heavy metal detoxification of Cd and Hg, lends itself naturally to the question of whether or not metal exchange in metalloproteins could lead to the incorporation of toxic Cd and Hg metal ions into essential proteins, causing severe physiologically consequences.
		For the most part, Cd-substituted metalloproteins are able to retain their biological activity and the high dispersion of the chemical shift range of 113Cd (over 900 ppm), results in an increased sensitivity to subtle differences in the coordination environment.
	www.uvm.edu /~swgordon/231-03/finprojects/Kay/KAYINOR.HTM (3272 words)

	Ask A Scientist - Metalloproteins
		The function of these metalloproteins and other chelators is partly to prevent the metal from forming unwanted complexes and precipitates (although I should note that copper and zinc tend to be soluble at the pH and chloride concentration normally found in the body).
		Many trace metals (although not zinc) are toxic to cells, so their concentrations must be carefully sensed and controlled.
		Metalloproteins can in some cases act as sensors and report the level of a metal ion to the cell so that appropriate homeostatic mechanisms can be triggered to raise or lower the metal ion to the necessary safe concentration.
	www.hhmi.org /cgi-bin/askascientist/highlight.pl?kw=&file=answers%2Fmolecular%2Fans_016.html (426 words)

	Research
		blue-copper, heme metalloproteins) at the level of the single molecule by means of scanning probe microscopy.
		Metalloproteins are used in this research activity as active elements of hybrid nanoelectronic devices.
		Particularly, in single protein transistors, a gate voltage swithches the current flow through a metalloprotein immobilized in a ~ 5 nm gap (made by state of the art electron beam lithography) by varying the alignement of the unoccupied molecular levels to the Fermi level of the leads.
	www.biophysics.unimo.it /Research.html (623 words)

	Research
		Metalloproteins are proteins that contain one or more transition metal ions at their active-sites, and can be thought of as the ultimate transition metal complex.
		One of the main reasons for this is that the complexity of metalloproteins often lends a systematic approach to studying structure/function relationships impractical.
		Currently we are interested in three distinct areas of research: metalloproteins that respond to oxidative stress (nickel superoxide dismutase and SoxR), coordination chemistries relevant to prion diseases, and electron transfer reactions performed by iron-sulfur proteins.
	web.mac.com /jasonshearer/iWeb/Site/Research.html (800 words)

	NMR of dinuclear metalloproteins
		Paramagnetic transition metal-containing metalloproteins can be studied by the use of a number of different magnetic and spectroscopic methods owing to the presence of unpaired electrons on the metal ions.
		Studies of metalloproteins with spectroscopically active metal ions as intrinsic or external probes have provided further insight into the coordination chemistry of the active site in metalloproteins, including the coordination geometry, the coordinated amino acid side chains, the status of the coordinated water, and substrate and inhibitor bindings.
		Particularly, NMR studies of paramagnetic metalloproteins, metallo-biomolecules, and synthetic chemical models have become a new advanture [15,18] In this review, we discuss the studies of several dinuclear metalloproteins by the use of 1D and 2D NMR techniques that have been accomplished in the past few years.
	chuma.cas.usf.edu /~ming/Publications/abstracts/abstract17.htm (1320 words)

	Wiley::Handbook of Metalloproteins, 2 Volume Set
		In recent years, the analysis and classification of metalloproteins at the interface between chemistry and biology has accelerated.
		Content is presented in both a large format and full colour and covers the most relevant transition metals such as Iron, Nickel, Copper, Cobalt, Molybdenum, Manganese Tungsten and Vanadium.
		This is the first Handbook of Metalloproteins ever published and is comprised of articles written by renowned experts in the field.
	www.wiley.com /WileyCDA/WileyTitle/productCd-0471627437.html (339 words)

	AcademicDB - Discuss the roles that the protein components play in the classes of metalloproteins.
		This document is part of AcademicDB, a database of over 15,000 UK university essays and coursework documents written by UK university students covering all subject areas.
		In any case the protein component of the metalloproteins plays significant roles, some of which are: 1.
		If you want immediate access to this document in full, and 15,000+ like it, you will need to either log in or register now.
	www.academicdb.com /discuss_roles_that_protein_components_play_the_cla_7002 (255 words)

	A high-throughput method for the detection of metalloproteins on a microgram scale -- Högbom et al., ...
		Proteins that bind transition metals make up a substantial portion of the proteome and the identification of a metal cofactor in a protein can greatly facilitate its functional assignment and help place it in the context of known cellular pathways.
		Existing methods for the detection of metalloproteins generally consume large amounts of protein, require expensive equipment, or are very labor intensive, rendering them unsuitable for use in high-throughput proteomics initiatives.
		Here we present a method for the identification of metalloproteins that contain iron, copper, manganese, cobalt, nickel, and/or zinc, that is sensitive, quick, robust, inexpensive, and can be performed with standard laboratory equipment.
	www.mcponline.org /cgi/content/abstract/T400023-MCP200v1 (294 words)

	The structure of metalloproteins in solution
		Metalloproteins are ubiquitous electron transfer proteins involved in fundamental biological processes such as photosynthesis, oxidative phosphorylation and nitrogen fixation (Sticht et al., 1995; Sticht & Rösch, 1998; Sticht, 1999).
		One project concentrates on the cytochrome c6 and the [2Fe-2S] ferredoxin from the thermophilic cyanobacterium Synechococcus elongatus which function as a electron donor and an electron acceptor for photosystem I (PSI), respectively (figure).
		The structure of this protein (Schweimer et al., submitted), which is the first known structure of an eukaryotic rubredoxin, revealed a surface potential that differs considerably from that found in prokaryotic rubredoxins.
	btcpxx.che.uni-bayreuth.de /Projekte/metallo2.html (540 words)

	Chemistry at BU - Inorganic Chemistry
		Research in Inorganic Chemistry spans the continuum from small molecule systems to metalloproteins, from the investigation of the reactivity properties of synthetic complexes to the use of metal-based reagents for probing protein-DNA interactions.
		Protein film voltammetry (PFV) is used in the Elliott lab as a way to explore the electron transfer pathways and redox-dependent catalytic chemistry of complex metalloproteins such as sulfite reductase and multicopper oxidases.
		We also are devloping proteomic tools to allow us to probe the 'metallome' -- a complete read-out of the metal-binding components of biological pathways -- such that we can develop new insight into the role of metal ions in biochemistry.
	www.bu.edu /chemistry/faculty/researchareas/inorganic.html (414 words)

	UofR Events: Show single event (Site not responding. Last check: 2007-10-11)
		The ET data obtained on model systems is of a great importance for elucidation of a sequence-structure-function relationship in more complex redox metalloproteins.
		In this respect, my research projects to be presented are focused on the ET studies in model synthetic metalloproteins.
		To understand the role played by the protein matrix in mediating redox processes, ET reaction across a well-defined hydrophobic non-covalent interface of the de novo designed coiled-coil motif has been studied by pulse radiolysis technique.
	www.uregina.ca /cgi-bin/WebEvent3.05/cals/webevent.cgi?cmd=listevent&ncmd=calmonth&cal=cal1&y=2006&m=02&d=2&id=1137423658-23791-1&token=&sb=0&cf=cal&lc=calmonth&swe=1&set=1&sa=0&sort=e,m,t&ws=0&sib=1 (219 words)

	Kemisk Institut Københavns Universitet Calendar
		The purpose of this study is to improve the methodology for applying nuclear magnetic resonance (NMR) in investigations of structure and function of metalloproteins.
		The methodology was primarily applied to the blue copper protein plastocyanin, where the geometric structure of the metal site coordination sphere and the unpaired electron spin distribution were determined by paramagnetic NMR.
		Subsequently, a simple description of the nucleus-electron interactions in metalloproteins by natural bond orbitals was developed that, in turn, will improve the methodology for determining the solution structure and function of metalloproteins by paramagnetic NMR.
	www.kiku.dk /inter/index.php?action=event&lang=EN&menu=calendar&act=1&id=2797 (104 words)

	A HINT TO SEARCH METALLOPROTEINS IN GENE BANKS (Site not responding. Last check: 2007-10-11)
		At present, there is a lack of specific tools to address the matter of the identification of metalloproteins in databases of gene sequences; using knowledge based on our experience in biological inorganic chemistry, we have developed a methodology for the identification of metalloproteins in genome databanks.
		Then, by measuring all distances between the metal atom(s) contained in the structure and the non-hydrogen atoms of the protein, the donor atoms are readily identified and thus the amino acids binding to the metal (i.e.
		The primary structure of the metalloprotein (the query) from the PDB and of the corresponding MBP are used as input for a variant of BLAST, PHI-BLAST to scan gene banks (or a complete genome sequence).
	www.cerm.unifi.it /Link1.html (379 words)

	Macromolecular Structure and Dynamics - 67Zn Solid-State NMR of Metalloproteins
		Zinc is found in relatively low abundance in nature, e.g., nominally 70 ppm in the earth’s crust and approximately 0.01 ppm in sea water (Frausto da Silva et al.
		Yet, zinc plays an essential role in biology in the form of zinc metalloproteins and as a regulatory agent in homeostasis.
		These data represent a novel means to characterize the structure and bonding associated with the Zn in a metalloprotein.
	www.emsl.pnl.gov /docs/annual_reports/msd/annual_report1999/1573b-2n.html (843 words)

	The identification of metal-binding ligand residues in metalloproteins using nuclear magnetic resonance spectroscopy -- ...
		The identification of metal-binding ligand residues in metalloproteins using nuclear magnetic resonance spectroscopy -- SCROFANI et al.
		The identification of metal-binding ligand residues in metalloproteins using nuclear magnetic resonance spectroscopy
		The identification of metal-binding ligands in metalloproteins is an
	www.proteinscience.org /cgi/content/abstract/7/11/2476 (182 words)

	FEBS Abstract
		The situation is even more acute in the case of metalloproteins, which quite often are not amenable to high throughput expression approaches for a variety of reasons including the fact that many of them require a specific “metal chaperone” which lower organisms may lack.
		Metalloproteins are expected to make up at least a third of the genome and worldwide effort is beginning to take shape for what has recently been referred to as “metallogenomics”.
		A variety of X-ray techniques [Protein Crystallography, Solution X-ray Scattering and X-ray Absorption Fine Structure (XAFS)] have proved very powerful in studying not only structure/function relationships in metalloproteins but also are proving unique in understanding misfunction of these proteins which quite often results in debilitating disease.
	www.blackwellpublishing.com /febsabstracts2005/abstract.asp?id=40338 (377 words)

	Cellular response of antioxidant metalloproteins in Cu/Zn SOD transgenic mice exposed to hyperoxia -- Levy et al. 281 ...
		Metalloproteins, such as ceruloplasmin, metallothionein, and ferritin, are well known for their critical role in metal homeostasis
		The mechanism by which the induction of these metalloproteins protects against acute oxidative stress is still unknown.
		The third metalloprotein we examined, ferritin, is characterized primarily as an iron storage protein (3).
	ajplung.physiology.org /cgi/content/full/281/1/L172 (5310 words)

	Librería Tirant Lo Blanch - Handbook of metalloproteins. Varios Autores.
		This is the first comprehensive handbook covering the major metalloproteins to be published.
		It will include a computer-modelled structure for each compound, with information on the sequence information, synthesis and spectroscopic properties, functional aspects as well as key chemical, biological, physical and medical properties of the compound described.
		The two-volume handbook will be focused but will also provide comprehensive coverage of each key metalloprotein making this an essential reference source for researchers in the area..
	www.tirant.es /detalle?articulo=0471627437&titulo=Handbook (131 words)

	Hendrich Metalloprotein Group (Site not responding. Last check: 2007-10-11)
		These and other metalloproteins are essential for the basic processes of life, including DNA synthesis, metabolism, photosynthesis, detoxification, and the chemical transformations of nitrogen, oxygen, and carbon molecules required for life.
		An understanding of the function of metalloproteins comes from both structural and spectroscopic studies of the chemical states of the metal centers when processing substrates.
		Two larger complexes under current study in the group are the b6f complex of oxygenic photosynthesis and a new class of multiheme enzymes important in metabolic functions.
	www.chem.cmu.edu /groups/hendrich (360 words)

	HML: A Multidisciplinary Approach for the Qualitative and Quantitative Determination of Metalloproteins used as Health ...
		The objective of this research is to improve analytical procedures for the identification and quantification of metalloproteins using hyphenated, mass spectrometric analytical measurement approaches.
		Since their discovery, metalloproteins have been the focus of research in biology and medicine because of their various functions in connection with protein folding and neurodegenerative diseases, metalloenzyme activity, and detoxification through transport and storage mechanisms.
		The desired outcome of this exploratory research is a cutting-edge set of screening and quantification strategies and new instrumental methods that assist with the quantification of metalloproteins.
	www.hml.noaa.gov /stressors/disease/markers.html (309 words)

	TSRI - News and Publications
		Metalloproteins make up a third of all proteins, and the same metal can have several diverse functions, depending on the protein component.
		We use high-resolution crystallography, advanced computer techniques, and protein engineering to understand the role of protein in controlling the properties of metals in biological systems.
		We plan to examine a series of these structures in different spin and oxidation states and to build a database of highly accurate metal-ligand parameters that heretofore were not available for iron metalloproteins.
	www.scripps.edu /news/sr/sr2000/mb04.html (718 words)

	MDB (Main Page) - Metalloprotein Site Database & Browser, TSRI
		November 06, 2001 - (Beta) Added a simple search interface showing the results of using the MSIT program to index metalloproteins.
		December 11, 2000 - Updated the MDB content using all structures from the PDB released as of Wednesday, December 6, 2000.
		This database is being developed as part of a project whose ultimate goal is metalloprotein design, allowing the interactive visualization of geometrical and functional information garnered from the MDB.
	metallo.scripps.edu (2151 words)

	Wiley::Handbook of Metalloproteins, 3 volume set
		The first two volumes of the "Handbook of Metalloproteins", published in 2001, focused on a number of metals, including iron, nickel, manganese, cobalt, copper and vanadium.
		Now we are delighted to present volume three which extends the wealth of knowledge and focuses on proteins found in the redox-inactive ions of zinc and calcium.
		The amazing new set will prove to be an essential reference providing comprehensive understanding and focused coverage of metalloproteins.
	eu.wiley.com /WileyCDA/WileyTitle/productCd-047086981X.html (225 words)

	Handbook on Metalloproteins
		This Handbook on Metalloproteins focuses on the available structural information of proteins and their metal ion coordination spheres.
		It centers on the metal ions indispensable for life but also considers metal ions used as substitution probes in studies of metalloproteins.
		Emphasizing the structure-function relationship, the book covers the common and distinct characterstics of metallo- enzymes, proteins, and amino acids bonded to copper, zinc, iron, and more.
	www.cplbookshop.com /contents/C1483.htm (136 words)

	Mike Ogawa Research
		Work being pursued in our group seeks to prepare a new class of synthetic metalloproteins which can mimic, enhance, or even expand the repertoire of chemical functions now being performed by natural metalloenzymes.
		We are particularly interested in designing “miniature metalloproteins” which possess novel photoactive properties for use in such applications as solar energy conversion, photodynamic tumor therapy, and drug delivery systems.
		Our approach to these problems begins with the use of solid-phase peptide synthesis to design self-assembling peptide structures which incorporate native-like metal-binding domains into their hydrophobic interiors in a manner similar to that found in naturally occurring metalloproteins (Figure 1).
	www.bgsu.edu /departments/chem/ogawa/research.html (473 words)

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