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Topic: Globular protein

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Hemoprotein

Hemoglobin

Artery

	Golbular Protein
		Globular proteins are relatively spherical in shape as the name implies.
		Hemoglobin consists of four protein chains and four heme groups that carry oxygen from the lungs to the tissue cells.
		The heme is held in position by the bonding of a nitrogen on a histidine side chain from the protein to iron in heme.
	www.elmhurst.edu /~chm/vchembook/568globularprotein.html (829 words)

	Electronic dissertations library
		Proteins are composed of 20 basic units called amino acids which consist of a central carbon atom (the alpha-carbon) bound to an amino group (NH2), a carboxyl group (COOH), a hydrogen atom, and one of 20 different R groups.
		Proteins are thought to initially fold rapidly into a structure in which most of the final secondary structure elements have formed and are aligned in roughly the correct way.
		Protein structure is often divided into four classes: ‘all-alpha‘ have only alpha-helical structures, ‘all-ß‘ have only ß-sheet structures, ‘alpha+ß;‘ have both alpha-helices and ß-sheets but the two types of structure are in different sections of the linear sequence, and ‘alpha/ß;‘ have both structures mixed along the protein chain (Levitt and Chothia (1976)).
	panizzi.shef.ac.uk /elecdiss/edl0002/proteina.html (2930 words)

	protein - HighBeam Encyclopedia
		Proteins are large molecules with high molecular weights (from about 10,000 for small ones [of 50-100 amino acids] to more than 1,000,000 for certain forms); they are composed of varying amounts of the same 20 amino acids, which in the intact protein are united through covalent chemical linkages called peptide bonds.
		Many globular protein molecules are easily crystallized and have been examined by X-ray diffraction, a technique that allows the visualization of the precise three-dimensional positioning of atoms in relation to each other in a crystal.
		Proteins are needed in the diet mainly for their amino acids, which the body uses to build new proteins (see nutrition).
	www.encyclopedia.com /doc/1E1-protein.html (905 words)

	Globular protein - Wikipedia, the free encyclopedia
		Globular proteins, or spheroproteins are one of the two main protein classes, comprising globelike proteins that are more or less soluble in aqueous solutions (where they form colloidal solutions).
		The term globular protein is quite old (dating probably from the 19th century) and is now somewhat archaic given the hundreds of thousands of proteins and more elegant and descriptive structural motif vocabulary.
		The spherical structure is induced by the proteins' primary structure.
	en.wikipedia.org /wiki/Globular_protein (292 words)

	Globular protein
		A globular protein is a protein that is globe-like, or rounded in shape, often soluble in aqueous solution.
		This distinguishes them from fibrous proteins[?], such as keratin, which may not be all that soluble.
		Among the most known globular proteins is hemoglobin, a member of the globin protein family[?].
	www.ebroadcast.com.au /lookup/encyclopedia/gl/Globular_protein.html (94 words)

	Globular Protein
		In a globular protein, the amino acid chain twists and folds in a manner that enhances the protein's solubility in water by placing polar groups of atoms at the protein's surface (where they can participate in attractive interactions with water molecules).
		The aqueous solubility of globular proteins allows them to exist in biological fluids as individual molecules or in small clusters and to accomplish a wide range of critical biological functions, for example, the enzymatic catalysis of chemical reactions.
		Globular proteins also function as anti-bodies in the body's immune system and as transport vehicles for other molecules in circulating blood, and they are heavily involved in the replication and repair of DNA.
	www.chemistryexplained.com /Ge-Hy/Globular-Protein.html (435 words)

	Process for making potato chip having no added fat or globular protein - Patent 5952026
		Prior to the invention, the protein coating was thought to be essential in the preparation of a potato chip by this process, and it was believed that the globular protein forms a translucent film on the surface of the potato chip to give the proper appearance, texture and color.
		The slice, not coated with globular protein, is then heated in a microwave oven for a period of time sufficient to produce a potato chip having substantially the same flavor, color and crispness as deep fat fried potato slices, yet having no added fat.
		globular protein) on the surface of the potato slices are necessary to achieve a desirable finished potato chip, using such potatoes as the starting material.
	www.freepatentsonline.com /5952026.html (5911 words)

	Designing a Novel Globular Protein Fold
		Protein function depends on the complex geometries assumed as sequences of amino acids (each comprising a carboxyl group, an amino group, and a side chain) link into chains of residues that form local structural units such as α helices and β strands, and finally fold into compact, three-dimensional, globular domains and multidomain structures.
		How proteins do this work depends on their three-dimensional structure, which is replete with folds, crevices, and other features that are just as important as the chemical composition specified by the recipe.
		First, it is a strong validation of the understanding and description of the energetics of proteins and other macromolecules, much of which, incidentally, has been a consequence of the determination of high-resolution structures of those macromolecules.
	www-als.lbl.gov /als/science/sci_archive/76globular_protein.html (975 words)

	Protein - Wikipedia, the free encyclopedia
		Proteins are large organic compounds made of amino acids arranged in a linear chain and joined together between the carboxyl atom of one amino acid and and the amine nitrogen of the other.
		The total complement of proteins present in a cell or cell type is known as its proteome, and the study of such large-scale data sets defines the field of proteomics, named by analogy to the related field of genomics.
		Consequently, numerous alternative theories of the protein primary structure were proposed, e.g., the colloidal hypothesis that proteins were assemblies of small molecules, the cyclol hypothesis of Dorothy Wrinch, the diketopiperazine hypothesis of Emil Abderhalden and the pyrrol/piperidine hyopthesis of Troensgard (1942).
	en.wikipedia.org /wiki/Protein (5514 words)

	PROGRAM - NATO Advanced Research Workshop
		However, the most essential distinction between different monomeric unit of proteins is that some of these units are hydrophobic, while others are hydrophilic or charged, thus in a very rough approximation it is possible to represent a globular protein as a kind of AB-copolymer.
		For proteins the corresponding sequences were selected in the course of molecular evolution, because otherwise globular enzymes would precipitate and would be unable to perform their biological functions.
		Typical snapshots of the globular structures for (a) protein-like, (b) random, and (c) random-block copolymers.
	www.cstl.nist.gov /nist831/NATO99/abstracts/khokl.html (1612 words)

	A ras Protein tutorial: Tufts University
		The Ras protein is a monomeric globular protein of 189 amino acids (21 kDa molecular mass) which is associated with the plasma membrane and which binds either GDP or GTP.
		This is a relatively small protein (177 amino acids) and the guanine nucleotide bound to the protein is shown as spacefilling to give you a sense of the relative size of a globular protein and a cofactor or substrate.
		Globular proteins are composed of distinct secondary structural elements folded back on one another to achieve an overall compact shape.
	ase.tufts.edu /biology/MolecVisual/bio152/rightrasD.html (1170 words)

	Proteins
		The primary structure of a segment of a polypeptide chain or of a protein is the amino-acid sequence of the polypeptide chain(s), without regard to spatial arrangement (apart from configuration at the alpha-carbon atom).
		However, most charged groups of proteins are on the surface of the protein where they do not strongly interact with other charged groups from the protein or other biopolymers due to the high dielectric constant of the water solvent, but are stabilized by hydrogen bonding and polar interactions to the water.
		The aggregation of protein subunits buries the hydrophobic residues of the proteins, and hence minimizes the number of thermodynamically unfavourable solute-solvent interactions as found when SWP is hydrated in distilled water at room temperature (Friedli, PhD thesis, chapter 3).
	www.friedli.com /herbs/phytochem/proteins.html (11287 words)

	Molecular motion and protein folding
		Protein folding can be studied in the test tube by dissolving a purified protein in aqueous solution and denature it using chaotropic agents which are polar and/or charged molecules.
		Proteins are micelle-like structures that consist of a hydrophobic core and a hydrophilic surface (globular proteins).
		The denaturation of proteins by decreasing the temperature, cold denaturation, is caused by the weakening of the hydrophobic effect (the entropy term of solvation).
	www.whatislife.com /reader/motion/motion.html (2505 words)

	Short yeast ORFs: expressed protein or not?
		Secondly, the false-positive rate (globular proteins predicted to contain membrane helices) of PHDhtm is particularly high for proteins with only one transmembrane helix [2], and only for 79 of the 550 proteins more than one membrane helix was detected (stronger predictions listed in the Appendix).
		Given the observed relation between protein length and the number of exposed residues, the difference between the number of exposed residues actually observed for a particular protein and that expected according to a fit to this relation (eqn.
		Assuming that most predictions for proteins with more than one membrane helix were correct, and that the ratio of proteins with one and two membrane helices in yeast is similar to that in other organisms, the conclusion was that about half of the proteins predicted to have one membrane helix were false positives.
	cubic.bioc.columbia.edu /papers/1999_globe/paper.html (3694 words)

	Biology 403: Protein Structure
		Some globular proteins, such as the globins and most cytochromes, are almost entirely helical; but even here the segments of alpha helix extend only for four to twenty amino acids, after which there is a turn or bend, and then another helix starts up.
		If a protein is highly similar in sequence to a protein whose structure has already been experimentally determined, then we can often successfully make the assumption that the unknown protein's structure will be nearly identical to that of the known protein.
		In a protein, where there are thousands of protons and hundreds of nitrogen atoms, the resonances are thoroughly overlapped, and even if one could separate out one of the resonances, assigning it to a specific atom-atom interaction would be impossible.
	www.csrri.iit.edu /~howard/biol403/proteinstructure.html (3962 words)

	PPS 96' - Tertiary Structure: Globular Proteins
		Most proteins which occur in the aqueous, intracellular environment or in the plasma are of globular nature: they are very approximately spherical in shape, or consist of several different lobes (domains).
		This is taken to extremes in a number of 'modular' proteins, which are mostly extracellular and glycosylated (see section on mosaic proteins).
		At a simple level, a globular protein may be considered to consist of a hydrophobic core surrounded by a hydrophilic external surface which interacts with water.
	www.cryst.bbk.ac.uk /PPS2/course/section10/globular.html (451 words)

	Protein Crystallization
		The importance of protein crystallization is that it serves as the basis for X-ray crystallography, wherein a crystallized protein is used to determine the protein’s three-dimensional structure via X-ray diffraction.
		Protein crystallization is inherently difficult because of the fragile nature of protein crystals.
		Both entail a droplet containing purified protein, buffer, and precipitant being allowed to equilibrate with a larger reservoir containing similar buffers and precipitants in higher concentrations.
	www.bio.davidson.edu /Courses/Molbio/MolStudents/spring2003/Kogoy/protein.html (1036 words)

	[No title]
		It teaches the student to recognize the main elements of protein secondary structure, and the main structural classes of globular proteins.
		Objectives The object of this exercise is to allow you to become familiar with the main architectural features of several classes of globular protein, by studying computer-generated interactive drawings of models of the proteins.
		Alpha/beta proteins: TIM and flavodoxin The final pair of proteins are a/b proteins, in which the secondary structural elements are alternating helices and strands of beta-sheet.
	www.umass.edu /microbio/rasmol/coulson.txt (2619 words)

	Radially Softening Diffusive Motions in a Globular Protein -- Dellerue et al. 81 (3): 1666 -- Biophysical Journal
		The characterization of internal diffusion in proteins is complicated by the variety of the motions present.
		The physical picture of a globular protein arising from the present analysis is as follows.
		Native proteins are surface-molten solids: application of the Lindemann criterion for the solid vs liquid state.
	www.biophysj.org /cgi/content/full/81/3/1666 (4048 words)

	HHMI News: Researchers Design and Build First Artificial Protein (Site not responding. Last check: )
		The ability to specify and design artificial proteins also opens the way for researchers to engineer artificial protein enzymes for use as medicines or industrial catalysts, said the study's lead author, Howard Hughes Medical Institute investigator David Baker at the University of Washington.
		Proteins are initially synthesized as long chains of amino acids and they cannot function properly until they fold into intricate globular structures.
		In their design and construction effort, the scientists chose a version of a globular protein of a type called an alpha/beta conformation that was not found in nature.
	www.hhmi.org /news/baker3.html (1200 words)

	Tertiary Protein
		Different protein chains or loops within a single chain are held together by the strong covalent disulfide bonds.
		In the prion protein, tyr 128 is hydrogen bonded to asp 178, which cause one part of the chain to be bonding with a part some distance away.
		The example on the left is from the prion protein with the salt bridge of glutamic acid 200 and lysine 204.
	www.elmhurst.edu /~chm/vchembook/567tertprotein.html (510 words)

	Proteins - structure and functions
		rhodopsin, membrane receptor proteins and acetylcholine or insulin.
		Proteins with common ancestors are often known as
		Unless protected during folding, proteins would interact with all the other molecules in a cell.
	fig.cox.miami.edu /~cmallery/255/255prot/255proteins.htm (1125 words)

	HEMP SEED: The Most Nutritionally Complete Food Source In The World
		Proteins are made of amino acid peptide chains in specific sequences.
		Since hemp seed protein is 65% globulin edistin, and also includes quantities of albumin, its protein is readily available in a form quite similar to that found in blood plasma.
		If the globulin protein starting material is in short supply the army of antibodies may be too small to prevent the symptoms of sickness from setting in.
	www.ratical.org /renewables/hempseed1.html (1793 words)

	To be folded or to be unfolded? -- Garbuzynskiy et al. 13 (11): 2871 -- Protein Science
		Histograms representing the distribution of 90 "natively unfolded" proteins (fl bars) and 80 "ideally" folded proteins (gray bars) as a function of (A) expected number of contacts, (B) hydrophobicity on the Kyte and Doolittle (1982) scale, (C) absolute magnitude of net charge, and (D) optimal set of artificial parameters.
		The dependence of the fraction of proteins predicted incorrectly (i.e., native proteins predicted as natively unfolded and vice versa) on the border position of considered parameters between two sets of proteins: (E) for expected number of contacts, (F) for hydrophobicity, (G) for absolute magnitude of net charge, and (H) for optimal set of artificial parameters.
		Wright, P.E. and Dyson, H.J. Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm.
	www.proteinscience.org /cgi/content/full/13/11/2871 (3027 words)

	Pex5p, the Peroxisomal Cycling Receptor, Is a Monomeric Non-globular Protein -- Costa-Rodrigues et al. 280 (26): 24404 ...
		Pex5p, the Peroxisomal Cycling Receptor, Is a Monomeric Non-globular Protein -- Costa-Rodrigues et al.
		globular protein upon size exclusion chromatography (27, 28).
		Pex5p, the GST fusion proteins, and the sedimentation standards are indicated by arrows.
	www.jbc.org /cgi/content/full/280/26/24404 (5387 words)

	What is Rosetta@home?
		Proteins are initially synthesized as long chains of amino acids and, for the most part, they cannot function properly until they fold into intricate globular structures.
		In CAPRI, predictors are given the structures of two proteins known to form a complex, and challenged to predict the structure of the complex.
		Our methods will be tested in upcoming CASP and CAPRI experiments and implemented in our publicly available protein structure prediction server, Robetta, which is currently used by hundreds of academic scientists from around the world for free, and has been shown to be one of the best fully-automated structure prediction servers in recent CASP experiments.
	boinc.bakerlab.org /rosetta/rah_about.php (916 words)

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