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Topic: Disulfide bridge

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	Disulfide bond
		A disulfide bond (SS-bond), also called a disulfide bridge, is a strong covalent bond between two sulfur atoms.
		Disulfide bonds play an imporant protective role for bacteria as a reversible switch that turns a protein on or off when bacterial cells are exposed to oxidation reactions.
		Disulfide bonds also play a significant role in the vulcanization of rubber.
	www.ebroadcast.com.au /lookup/encyclopedia/di/Disulfide_bridge.html (204 words)

	Disulfide bond - Wikipedia, the free encyclopedia
		Disulfide bonds are usually formed from the oxidation of sulfhydryl (-SH) groups, as depicted formally in Figure 1.
		Disulfide bonds in proteins are formed between the thiol groups of cysteine residues.
		The prototype of a protein disulfide bond is the two-amino-acid peptide, cystine, which is composed of two cysteine amino acids joined by a disulfide bond (shown in Figure 2 in its unionized form).
	en.wikipedia.org /wiki/Disulfide_bridge (1362 words)

	BioMed Central \| Full text \| The effect of engineered disulfide bonds on the stability of Drosophila ...
		Disulfide bonds are present in most extracellular proteins, where they presumably stabilize the native conformation by lowering the entropy of the unfolded form [11] or by decreasing the unfolding rate of irreversibly denatured proteins [12,13].
		All these 7 disulfide bonds were predicted by MODIP, automated software for modeling disulfide bonds in proteins [19] with grades A (ideal stereochemistry), B (geometrically suitable but with distorted stereochemistry) and C (sites close enough to allow the formation of a disulfide bond) [20].
		This instability has been interpreted as the result of atypical sets of dihedral angles in newly formed disulfide bridges [37], from stabilization of the denatured state [38] or from reduction of disulfide bonds followed by disulfide exchange or chemical reaction of the SH groups formed [39,40].
	www.biomedcentral.com /1471-2091/7/12 (3043 words)

	Disulfide Bridge Engineering in the Tachykinin NK1 Receptor
		Cys residues were introduced in the N-terminal extension and in the third extracellular loop, respectively, in such a way that disulfide bridge formation could be monitored by loss of substance P binding and breakage of the bridge could be monitored by gain of ligand binding.
		This disulfide bridge formed spontaneously in the whole population of receptors and could be titrated with low concentrations of reducing agent, dithiothreitol.
		It is concluded that disulfide bridges form readily between Cys residues introduced appropriately in the N-terminal extension and the third extracellular loop, whereas they form with more difficulty between Cys residues placed at the extracellular ends of the transmembrane segments even at positions where high-affinity metal ion sites can be constructed with His residues.
	pubs.acs.org /cgi-bin/abstract.cgi/bichaw/2000/39/i04/abs/bi991777b.html (305 words)

	the fifth disulfide bridge (Site not responding. Last check: 2007-11-03)
		The homolog I used is an agatoxin (PDB ID 1eit) that has 8 residues of cysteine forming 4 disulfide bridges.
		The protein of unknown structure has 10 residues of cysteine and therefore has the ability to form a fifth disulfide bridge.
		Here is a comparison of the resulting structures when the fifth disulfide bridge is created or not.
	maven.smith.edu /~vvouille/agoucenter.html (124 words)

	Ziconotide - Article Summaries (via CobWeb/3.1 planetlab2.cs.unc.edu) (Site not responding. Last check: 2007-11-03)
		Synthetic versions of seven naturally occurring omega-conopeptides were subjected to structural analyses in order to determine their disulfide bridge pattern.
		All synthetic peptides, SNX-111, -157, -159, -183, -185, -230 and -231, were found to have the same disulfide bridge pattern as determined for the naturally occurring omega-conopeptide G-VI-A, i.e.
		disulfide bridges between the half-cystines 1-16, 8-20 and 15-25 (using the amino-acid numbering of SNX-111).
	docmd.com.cob-web.org:8888 /Ziconotide/artsum.asp?artnumber=11 (171 words)

	The Role of Dimerization in Prion Replication -- Tompa et al. 82 (4): 1711 -- Biophysical Journal
		is a dimer with stabilizing intermolecular disulfide bridges (Fig.
		Effect of the disulfide bridge and the C-terminal extension on the oligomerization of the amyloid peptide ABri implicated in familial British dementia.
		The role of disulfide bridge in the folding and stability of the recombinant human prion protein.
	www.biophysj.org /cgi/content/full/82/4/1711 (3904 words)

	Disulfide bond (via CobWeb/3.1 planetlab2.cs.unc.edu) (Site not responding. Last check: 2007-11-03)
		A disulfide bond ('''SS-bond'''), also called a disulfide bridge, is a strong covalent bond between two sulfhydryl groups.
		In eukaryotic cells, disulfide bonds are formed in the lumen of the RER (rough endoplasmic reticulum) but not in the cytosol.
		Thus disulfide bonds are found only in secretory proteins, lysosomal proteins, and the exoplasmic domains of membrane proteins.
	disulfide-bond.iqnaut.net.cob-web.org:8888 (430 words)

	Transcription and Translation Worksheet (Site not responding. Last check: 2007-11-03)
		The two subunits are held together by two interchain disulfide bridges.
		In addition, there is an intrachain disulfide bridge in the A chain.
		The protein is synthesized initially as a single polypeptide of 105 amino acids and the first 24 amino acids serve as a signal peptide for secretion.
	www.msu.edu /course/lbs/145/smith/s02/trans_worksheet.html (364 words)

	Hindered linking agents and methods - Patent 5183904
		In the present invention, an aromatic disulfide compound may be reacted with the immunoglobulin and the substituted 2-iminothiolane hydrohalide prior to reaction with the toxin.
		The presence of an aromatic disulfide in the immunoglobulin/2IT reaction mixture (i) allows real-time monitoring of the progress and extent of the reaction, (ii) activates the exposed sulfhydryl, and (iii) blocks reactive sulfhydryls in the immunoglobulin, preventing antibody dimerization prior to and during the subsequent reaction with the toxin.
		The relative increase in disulfide stability (or, the relative rate reduction) of the substituted 2-iminothiolanes compared to unsubstituted 2-iminothiolane and to SPDP is presented in Table D. It was measured by dividing the rate constant for unsubstituted 2-iminothiolane (9.42.times.10.sup.-3) by that for each of the substituted 2-iminothiolanes.
	www.freepatentsonline.com /5183904.html (6340 words)

	Formation of Disulfide Bridges by a Single-chain Fv Antibody in the Reducing Ectopic Environment of the Plant Cytosol ...
		Disulfide bridge formation in the reducing environment of the cytosol is considered a rare event and is mostly linked to inactivation
		presence of disulfide bridges in the in planta-expressed scFv
		The capability of a scFv antibody to form disulfide bridges in the cytosol is remarkable.
	www.jbc.org /cgi/content/full/277/22/19339 (4910 words)

	Michigan GI Peptide Research Center
		Disulfide bond formation is either performed post-assembly on-resin or post synthesis in solution using the deprotected and purified peptide as reviewed recently by Andreu and Annis [17,18].
		The first (or only) disulfide bridge is most easily created by air oxidation of the fully deprotected peptide in aqueous basic buffers at room temperature.
		If more than one disulfide bridge is to be formed, the additional Cysteine-pair is incorporated during solid phase synthesis carrying an independently removable protecting group, stable to the conditions of synthesis and resin cleavage.
	www.med.umich.edu /mgpc/cores/ppc.htm (2061 words)

	Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme -- JACOBSON et al. ...
		Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme -- JACOBSON et al.
		Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme
		The engineered disulfide bridge between residues 21 and 142 of phage T4 lysozyme spans the active-site cleft and can be used as a switch to control
	www.proteinscience.org /cgi/content/abstract/1/1/46 (523 words)

	Proteins - Tertiary Structure (Site not responding. Last check: 2007-11-03)
		Disulfide bonds are formed in an oxidizing environment between cysteine residues in different parts of a protein chain:
		The influenza virus haemaglutinin protein is another structure in which disulfide bonds stabilize a conformation wildly different than expected.
		The looped-out sections of chain contain the antigenic regions; amino acid mutations in these regions alter the antigenic character of the molecule, resulting in the recurring influenza epidemics with which we all are familiar.
	chemistry.umeche.maine.edu /CHY431/Proteins11.html (458 words)

	Sindbis Virus Glycoprotein E1 Is Divided into Two Discrete Domains at Amino Acid 129 by Disulfide Bridge Connections -- ...
		Although no direct disulfide bonds were determined, E1 1 to 129 can be cleaved chemically and digested into at least thee peptides under conditions where the disulfides in this region remain intact.
		Sindbis virus membrane fusion is mediated by reduction of glycoprotein disulfide bridges at the cell surface.
		Disulfide bonds are essential for the stability of the Sindbis virus envelope.
	jvi.asm.org /cgi/content/full/74/19/9313 (2323 words)

	BioMed Central \| Full text \| A two disulfide bridge Kazal domain from Phytophthoraexhibits stable inhibitory activity ...
		However, a novel class of Kazal domains with two disulfide bridges resulting from the absence of the third and sixth cysteines have been found in biologically important molecules, such as human LEKTI, a 15-domain inhibitor associated with the severe congenital disease Netherton syndrome.
		The finding that the two disulfide bridge atypical Kazal domain EPI1a is a stable inhibitor indicates that the missing two cysteines and their corresponding disulfide bond are not essential for inhibitor reactivity and stability.
		The lack of one disulfide bond and the longer sequence stretch between the first two cysteines were proposed to be the factors responsible for the instability of LD6 [11].
	www.biomedcentral.com /1471-2091/6/15 (5280 words)

	Exercise Four - BPTI
		Exercise Four introduces tertiary structure, and specifically examines the role of disulfide bridges and the hydrophobic core in stabilizing the folded conformation of BPTI.
		The disulfide bridges are shown in yellow, the beta strands in green and the alpha helices in red.
		In addition, three disulfide bonds are formed in the stable fold, linking cysteines 5 and 55, 14 and 38 and 30 and 51.
	www.cgl.ucsf.edu /home/glasfeld/tutorial.SAVE/bpti/bpti.html (1472 words)

	Glyceraldehyde 3-phosphate dehydrogenase
		There is a disulfide bridge between Cys 123 and Cys 149, the two red colored cysteines (on each chain):
		This disulfide bond is not seen in other archaeal GAPDH, but it seems to provide structural stability holding together alpha helix 138-153 of the catalytic domain and a short alpha helix 120-125 from the NAD binding domain; this may help provide thermostability.
		Disulfide bonds are usually uncommon in intracellular enzymes.
	www.stanford.edu /~mmogri/bio/gapdh/structure2.html (322 words)

	FeatureMap3D 1.0 Usage instructions
		If, for example, a disulfide bridge at positions 231 and 249 were to be shown in white stick representation, the user would enter
		if he wishes to show the disulfide bridge as yellow sticks instead - the codes are only used to specify a certain color and representation and the program does not use the information about which type of annotation is to be shown.
		disulfide bridges can be annotated to "X" to mark the positions in white stick representation or "A" to use yellow stick representation).
	www.cbs.dtu.dk /services/FeatureMap3D/instructions.php (1483 words)

	An engineered disulfide bridge mimics the effect of calcium to protect neutral protease against local unfolding -- ... (Site not responding. Last check: 2007-11-03)
		An engineered disulfide bridge mimics the effect of calcium to protect neutral protease against local unfolding -- Dürrschmidt et al.
		An engineered disulfide bridge mimics the effect of calcium to protect neutral protease against local unfolding
		Owing to the presence of the disulfide bridge, the
	content.febsjournal.org /cgi/content/abstract/272/6/1523 (312 words)

	A C-Terminal Disulfide Bridge in Pediocin-Like Bacteriocins Renders Bacteriocin Activity Less Temperature Dependent and ...
		A C-Terminal Disulfide Bridge in Pediocin-Like Bacteriocins Renders Bacteriocin Activity Less Temperature Dependent and Is a Major Determinant of the Antimicrobial Spectrum -- Fimland et al.
		A C-Terminal Disulfide Bridge in Pediocin-Like Bacteriocins Renders Bacteriocin Activity Less Temperature Dependent and Is a Major Determinant of the Antimicrobial Spectrum
		Assignment of the disulfide bridges is based on studies by Henderson et al.
	jb.asm.org /cgi/content/full/182/9/2643 (3573 words)

	TERTIARY STRUCTURE
		The interactions in proteins that maintain structure cover the spectrum of chemical interactions from the covalent bonds of the amide backbone and the disulfide bridge through very polar charge-charge interactions to a variety of weaker, short distance interactions.
		The tertiary structure of proteins is characterized by tightly folded structure with polar groups on the surface and non-polar groups buried.
		Consider wheat germ agglutinin, where 16 turns (in cyan) and 16 disulfide bonds (in brown) are the predominant structural contributions.
	bmbiris.bmb.uga.edu /wampler/tutorial/prot3.html (993 words)

	Class Definition for Class 930 - PEPTIDE OR PROTEIN SEQUENCE
		(7) Compounds containing a cys-cys disulfide bridge between nonadjacent cysteine residues are placed in art collection 280 with the exception of those compounds such as atrial natriuretic peptide, vasopressin, or others containing disulfide bridges which are appropriate for art collection 40-170.
		for a compound with an interchain disulfide bridge.
		Subject matter under cross-reference art collection 10 containing peptides or proteins containing a cys-cys disulfide bridge between nonadjacent cysteine residues such as in the case of at least one intrachain disulfide bridge (cyclic) or at least one interchain disulfide bridge.
	www.uspto.gov /go/classification/uspc930/defs930.htm (4959 words)

	Disruption of the {beta}3 663-687 disulfide bridge confers constitutive activity to {beta}3 integrins -- Butta et al. ... (Site not responding. Last check: 2007-11-03)
		Disruption of the {beta}3 663-687 disulfide bridge confers constitutive activity to {beta}3 integrins -- Butta et al.
		disulfide bridge and shortening of the carboxy-terminal ectodomain
		A mutation in the extracellular cysteine-rich repeat region of the beta3 subunit activates integrins alphaIIbbeta3 and alphavbeta3.
	www.bloodjournal.org /cgi/content/full/102/7/2491 (3333 words)

	Vicinal disulfide turns -- Carugo et al. 16 (9): 637 -- Protein Engineering Design and Selection
		The disulfide bond formed between the side chains of adjacent
		In Figure 1 the structure of the vicinal disulfides is compared
		A few disulfide bonds are indicated with dashed lines.
	peds.oxfordjournals.org /cgi/content/full/16/9/637 (1097 words)

	The role of cysteine residues in structure and enzyme activity of a maize {beta}-glucosidase -- Rotrekl et al. 266 (3): ... (Site not responding. Last check: 2007-11-03)
		disulfide bridge at pH 8 spontaneously by a disulfide interchange
		we conclude that the disulfide bridge stabilizing the catalytically
		disulfide bridge involved in dimer structure stabilization is
	content.febsjournal.org /cgi/content/full/266/3/1056 (4326 words)

	Re: modeling disulfide without template (via CobWeb/3.1 planetlab2.cs.unc.edu) (Site not responding. Last check: 2007-11-03)
		Hi Tom, I wonder why it happens that an experimentally established disulfide bond is not confirmed in several crystal structures.
		Maybe the crystallization condition were not oxidative to support disulfide bridge formation.
		In this modeling case the template selection step must be crucial: a structure with a disulfide bridge, even if the structure itself is not the highest resolution one available, should enjoy priority.
	salilab.org.cob-web.org:8888 /archives/modeller_usage/2001/msg00074.html (203 words)

	CysView - Automated Protein Classification by Disulfide Connectivity Patterns
		CysView is a tool facilitating the grouping of entries in a database (Swissprot or GenBank format-based) by similar disulfide bridge patterns, 'disulfide connectivity patterns'.
		CysView searches through a flat file of multiple entries for information on disulfide pairing and returns a plot of disulfide bridges for entries that display the information.
		Entries with similar disulfide bridge pattern are grouped together.
	research.i2r.a-star.edu.sg /CysView (244 words)

	Spartanburg SC \| GoUpstate.com \| Spartanburg Herald-Journal (Site not responding. Last check: 2007-11-03)
		For example, the des [1] disulfide species has all the native disulfide bonds except that between cysteines 40 and 95.
		Disulfide bonds play an important protective role for bacteria as a reversible switch that turns a protein on or off when bacterial cells are exposed to oxidation reactions.
		for example the conversion of di-o-nitrophenyl disulfide to o-nitrophenylsulfur chloride Organic Syntheses, Coll.
	www.goupstate.com /apps/pbcs.dll/section?category=NEWS&template=wiki&text=disulfide_bridge (1318 words)

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