Test probe - Revision history

en>Materialscientist: Reverted 1 good faith edit by 122.167.4.137 using STiki

2014-10-14T09:57:08Z

Reverted 1 good faith edit by 122.167.4.137 using STiki

← Older revision		Revision as of 11:57, 14 October 2014
Line 1:		Line 1:
	~~Greetings!~~ I am ~~Marvella~~ and ~~I really feel comfortable when people use the complete title~~. ~~Doing ceramics~~ is ~~what~~ my ~~family~~ and I appreciate. ~~Minnesota~~ is ~~where~~ he'~~s been living for years~~. ~~He utilized to~~ be ~~unemployed but now he is a meter reader~~.<br><br>my blog ~~...~~ [http://~~3bbc~~.~~com~~/~~index.php~~?do=~~/profile-548128/info/~~ http://~~3bbc~~.com~~/index.php?do=~~/profile-~~548128~~/info/]		I would like to introduce myself to you, I am Andrew and my wife doesn't like it at all. Distributing production is exactly where my main earnings comes from and it's something I really appreciate. One of the extremely very best issues in the globe for him is doing ballet and he'll [http://www.prograd.Uff.br/novo/facts-about-growing-greater-organic-garden live psychic reading] be beginning something else alongside with it. My wife and I reside in Mississippi and I adore each working day residing here.<br><br>My blog post: accurate [http://galab-work.cs.pusan.ac.kr/Sol09B/?document_srl=1489804 psychic phone] predictions [[http://www.indosfriends.com/profile-253/info/ indosfriends.com]]

en>Glrx: /* Passive probes */ move new citation to later; template citation

2014-02-21T23:41:10Z

Passive probes: move new citation to later; template citation

← Older revision		Revision as of 01:41, 22 February 2014
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	~~'''Franz Hofmeister''' (1850–1922) was an early protein scientist,~~ and ~~is famous for his studies of salts that influence~~ the ~~solubility and conformational stability of [[protein]]s~~. ~~Hofmeister was the first to propose that polypeptides were [[amino acid]]s linked by [[peptide bond]]s in 1902, although this model of protein [[primary structure]] was independently~~ and ~~simultaneously conceived by [[Hermann Emil Fischer\|Emil Fischer]]~~.		Greetings! I am Marvella and I really feel comfortable when people use the complete title. Doing ceramics is what my family and I appreciate. Minnesota is where he's been living for years. He utilized to be unemployed but now he is a meter reader.<br><br>my blog ... [http://3bbc.com/index.php?do=/profile-548128/info/ http://3bbc.com/index.php?do=/profile-548128/info/]

	~~==Early life==~~
	~~Hofmeister's father was a doctor in Prague,~~ where ~~Hofmeister first began his studies, under the physiologist [[Karl Hugo Huppert]], himself a student of Carl Lehmann. Hofmeister~~'s ~~''Habilitationsschrift'' in 1879 concerned the peptic products of digestion~~.

	~~Hofmeister became professor of Pharmacology in [[Karl-Ferdinands-Universität\|Prague]] in 1885, then moved~~ to ~~Strasbourg in 1896.~~

	~~==The Hofmeister series==~~
	~~{{main\|Hofmeister series}}~~

	Hofmeister discovered a series of salts that have consistent effects on the solubility of proteins and (it was discovered later) on the stability of their [[secondary structure\|secondary]] and [[tertiary structure]]. Anions appear to have a larger effect than cations, and are usually ordered

	~~:<math>~~
	~~\mathrm{F^{-} \approx SO_{4}^{2-} > HPO_{4}^{2-} > acetate > Cl^{-} > NO_{3}^{-} > Br^{-} > ClO_{3}^{-} > I^{-} > ClO_{4}^{-} > SCN^{-}}~~
	~~</math>~~

	~~(This~~ is a ~~partial listing; many more salts have been studied~~.)
	~~The order of cations is usually given as~~

	:<~~math>~~
	~~\mathrm{NH_{4}^{+} > K^{+} > Na^{+} > Li^{+}~~ > ~~Mg^{2+} > Ca^{2+} > guanidinium}~~
	<~~/math>~~

	~~The mechanism of the Hofmeister series is not entirely clear, but seems to result mainly from effects on the solvent at higher salt concentrations (~~> ~~100 mM)~~. Early members of the series increase solvent surface tension and decrease the solubility of nonpolar molecules (''salt out''); in effect, they ''strengthen'' the [[hydrophobic interaction]]. By contrast, later salts in the series increase the solubility of nonpolar molecules (''salt in'') and decrease the order in water; in effect, they ''weaken'' the [[hydrophobic effect]]. However, these salts also interact directly with proteins (which are charged and have strong dipole moments) and may even bind specifically (e.g.~~, phosphate and sulfate binding to~~ [~~[ribonuclease A]]). Ions that have a strong ''[[salting in]]'' effect such as I<sup>−<~~/~~sup> and SCN<sup>−<~~/~~sup> are strong denaturants, because they salt in the peptide group, and thus interact much more strongly with the unfolded form of a protein than with its native form~~. ~~Consequently, they ''pull'' the unfolding reaction~~.~~<ref name~~="baldwin">{{cite journal \|author=Baldwin RL. \|title=How Hofmeister ion interactions affect protein stability \|journal=Biophys J \|volume=71 \|issue=4 \|pages=2056–63 \|year=1996 \|pmid=8889180 \|doi=10.1016/~~S0006-3495(96)79404-3 \|pmc=1233672 \|bibcode=1996BpJ....71.2056B}}</ref> Moreover, they may have direct interactions with some standard hydrophobic molecules, e.g., [[benzene]].~~

	~~==Protein purification==~~
	The importance of the Hofmeister series to early protein work cannot be underestimated, since it provided the chief tool for purifying proteins (sulfate precipitation) over the next ~50 years, one that is still in use today. Hofmeister himself may have been the first to crystallize a protein, hen egg-white albumin. Repeated crystallization was a favorite purification technique in the early days of protein science, and was essential for its development.

	~~==Proposal of protein primary structure==~~
	~~Hofmeister argued for peptide bonds by process of elimination. C-C, ether and ester bonds were unlikely considering the digestion by [[trypsin]]. R=C-N~~-~~C=R bonds could be eliminated because it would imply a much larger number of [[carboxylate]] groups than is observed experimentally.~~

	~~Hofmeister also argued for peptide bonds based on the [[biuret reaction]] observed with all proteins but never with free amino acids. Since [[biuret]] has the formula NH<sub>2<~~/~~sub>-CO-NH-CO-NH<sub>2<~~/~~sub>, that suggested the presence of similar peptide bonds in proteins.~~

	~~==See also==~~
	* [[primary structure]]
	* [[peptide bond]]
	* [http://~~www.scienceandsociety.co~~.uk/~~results~~.~~asp~~?~~image~~=~~10323274 Picture of Hofmeister at Science and Society site, UK]~~
	* [http://~~www.cendigital.org/cendigital/20120716?sub_id=FNQ5wyPIC7Sq&folio=42#pg46 Hofmeister Still Mystifies, ''Chemical & Engineering News'', July 16, 2012.]~~

	~~==References==~~
	~~<references/>~~
	* Hofmeister F. (1888) ''Arch. Exptl. Pathol. Pharmakol.'', '''24''', 247.
	*{{cite journal \| pmid = 17035073 \| doi=10.1016/j.cbpa.2006.09.020 \| volume=10 \| issue=6 \| title=Interactions between macromolecules and ions: The Hofmeister series \|date=December 2006 \| pages=658–63 \| last1 = Zhang \| first1 = Y \| last2 = Cremer \| first2 = P \| journal = Current Opinion in Chemical Biology}}
	*{{cite journal \| pmid = 16044460 \| doi=10.1002/prot.20500 \| volume=61 \| issue=1 \| title=Interactions of macromolecules with salt ions: an electrostatic theory for the Hofmeister effect \|date=October 2005 \| pages=69–78 \| last1 = Zhou \| first1 = Huan-Xiang \| journal = Proteins: Structure, Function, and Bioinformatics}}
	* Tanford C and Reynolds J. (2001) ''Nature's robots: a history of proteins'', Oxford University Press. ISBN 0-19-850466-7
	* Creighton TE. (1993) ''Proteins'', 2nd ed., W. H. Freeman. ISBN 0-7167-2317-4
	* Jencks WP. (1969) ''Catalysis in Chemistry and Enzymology'', Dover republication (1987). ISBN 0-486-65460-5
	* {{cite journal \| last1 = Collins \| first1 = KD. \| last2 = Washabaugh \| first2 = MW. \| year = 1985 \| title = The Hofmeister effect and the behaviour of water at interfaces \| url = \| journal = Q Rev Biophys \| volume = 18 \| issue = 4\| pmid = 3916340 \| pages = 323–422 }}

	~~{{See also\|Hofmeister (disambiguation){{!}}Hofmeister}}~~

	~~{{Persondata <!-- Metadata: see [[Wikipedia:Persondata]]. -->~~
	~~\| NAME = Hofmeister, Franz~~
	~~\| ALTERNATIVE NAMES =~~
	~~\| SHORT DESCRIPTION = German scientist~~
	~~\| DATE OF BIRTH = 1850~~
	~~\| PLACE OF BIRTH = [[Prague]]~~
	~~\| DATE OF DEATH = 1922~~
	~~\| PLACE OF DEATH =~~
	}}
	~~{{DEFAULTSORT:Hofmeister, Franz}}~~
	~~[[Category:1850 births]]~~
	~~[[Category:1922 deaths]]~~
	~~[[Category:19th-century German people]]~~
	~~[[Category:20th-century German people]]~~
	~~[[Category:19th-century Czech people]]~~
	~~[[Category:19th-century chemists]]~~
	~~[[Category:20th-century chemists]]~~
	~~[[Category:German chemists]]~~
	~~[[Category:Czech chemists]]~~
	~~[[Category:German biochemists]]~~
	~~[[Category:German people of German Bohemian descent]]~~
	~~[[Category:German Bohemian people]]~~
	~~[[Category:People from Prague]~~]

en>ClueBot NG: Reverting possible vandalism by 14.97.18.10 to version by Excirial. False positive? Report it. Thanks, ClueBot NG. (1670587) (Bot)

2014-01-27T04:00:59Z

Reverting possible vandalism by 14.97.18.10 to version by Excirial. False positive? Report it. Thanks, ClueBot NG. (1670587) (Bot)

← Older revision		Revision as of 06:00, 27 January 2014
Line 1:		Line 1:
	~~Hello~~. ~~Let me introduce~~ the ~~author~~. ~~Her name is Emilia Shroyer but it~~'s ~~not~~ the ~~most feminine name out there~~. ~~Puerto Rico is where he~~'s usually been ~~residing~~ but ~~she requirements~~ to ~~transfer simply~~ because of ~~her family members~~. ~~To collect cash~~ is 1 of the ~~issues I adore most~~. ~~Supervising~~ is ~~my profession~~.<br><br>~~My website~~ - [http://~~btcsoc~~.~~com~~/~~index~~.~~php~~?do=/~~profile-4621~~/~~info~~/ at ~~home std test~~]		'''Franz Hofmeister''' (1850–1922) was an early protein scientist, and is famous for his studies of salts that influence the solubility and conformational stability of [[protein]]s. Hofmeister was the first to propose that polypeptides were [[amino acid]]s linked by [[peptide bond]]s in 1902, although this model of protein [[primary structure]] was independently and simultaneously conceived by [[Hermann Emil Fischer\|Emil Fischer]].

			==Early life==
			Hofmeister's father was a doctor in Prague, where Hofmeister first began his studies, under the physiologist [[Karl Hugo Huppert]], himself a student of Carl Lehmann. Hofmeister's ''Habilitationsschrift'' in 1879 concerned the peptic products of digestion.

			Hofmeister became professor of Pharmacology in [[Karl-Ferdinands-Universität\|Prague]] in 1885, then moved to Strasbourg in 1896.

			==The Hofmeister series==
			{{main\|Hofmeister series}}

			Hofmeister discovered a series of salts that have consistent effects on the solubility of proteins and (it was discovered later) on the stability of their [[secondary structure\|secondary]] and [[tertiary structure]]. Anions appear to have a larger effect than cations, and are usually ordered

			:<math>
			\mathrm{F^{-} \approx SO_{4}^{2-} > HPO_{4}^{2-} > acetate > Cl^{-} > NO_{3}^{-} > Br^{-} > ClO_{3}^{-} > I^{-} > ClO_{4}^{-} > SCN^{-}}
			</math>

			(This is a partial listing; many more salts have been studied.)
			The order of cations is usually given as

			:<math>
			\mathrm{NH_{4}^{+} > K^{+} > Na^{+} > Li^{+} > Mg^{2+} > Ca^{2+} > guanidinium}
			</math>

			The mechanism of the Hofmeister series is not entirely clear, but seems to result mainly from effects on the solvent at higher salt concentrations (> 100 mM). Early members of the series increase solvent surface tension and decrease the solubility of nonpolar molecules (''salt out''); in effect, they ''strengthen'' the [[hydrophobic interaction]]. By contrast, later salts in the series increase the solubility of nonpolar molecules (''salt in'') and decrease the order in water; in effect, they ''weaken'' the [[hydrophobic effect]]. However, these salts also interact directly with proteins (which are charged and have strong dipole moments) and may even bind specifically (e.g., phosphate and sulfate binding to [[ribonuclease A]]). Ions that have a strong ''[[salting in]]'' effect such as I<sup>−</sup> and SCN<sup>−</sup> are strong denaturants, because they salt in the peptide group, and thus interact much more strongly with the unfolded form of a protein than with its native form. Consequently, they ''pull'' the unfolding reaction.<ref name="baldwin">{{cite journal \|author=Baldwin RL. \|title=How Hofmeister ion interactions affect protein stability \|journal=Biophys J \|volume=71 \|issue=4 \|pages=2056–63 \|year=1996 \|pmid=8889180 \|doi=10.1016/S0006-3495(96)79404-3 \|pmc=1233672 \|bibcode=1996BpJ....71.2056B}}</ref> Moreover, they may have direct interactions with some standard hydrophobic molecules, e.g., [[benzene]].

			==Protein purification==
			The importance of the Hofmeister series to early protein work cannot be underestimated, since it provided the chief tool for purifying proteins (sulfate precipitation) over the next ~50 years, one that is still in use today. Hofmeister himself may have been the first to crystallize a protein, hen egg-white albumin. Repeated crystallization was a favorite purification technique in the early days of protein science, and was essential for its development.

			==Proposal of protein primary structure==
			Hofmeister argued for peptide bonds by process of elimination. C-C, ether and ester bonds were unlikely considering the digestion by [[trypsin]]. R=C-N-C=R bonds could be eliminated because it would imply a much larger number of [[carboxylate]] groups than is observed experimentally.

			Hofmeister also argued for peptide bonds based on the [[biuret reaction]] observed with all proteins but never with free amino acids. Since [[biuret]] has the formula NH<sub>2</sub>-CO-NH-CO-NH<sub>2</sub>, that suggested the presence of similar peptide bonds in proteins.

			==See also==
			* [[primary structure]]
			* [[peptide bond]]
			* [http://www.scienceandsociety.co.uk/results.asp?image=10323274 Picture of Hofmeister at Science and Society site, UK]
			* [http://www.cendigital.org/cendigital/20120716?sub_id=FNQ5wyPIC7Sq&folio=42#pg46 Hofmeister Still Mystifies, ''Chemical & Engineering News'', July 16, 2012.]

			==References==
			<references/>
			* Hofmeister F. (1888) ''Arch. Exptl. Pathol. Pharmakol.'', '''24''', 247.
			*{{cite journal \| pmid = 17035073 \| doi=10.1016/j.cbpa.2006.09.020 \| volume=10 \| issue=6 \| title=Interactions between macromolecules and ions: The Hofmeister series \|date=December 2006 \| pages=658–63 \| last1 = Zhang \| first1 = Y \| last2 = Cremer \| first2 = P \| journal = Current Opinion in Chemical Biology}}
			*{{cite journal \| pmid = 16044460 \| doi=10.1002/prot.20500 \| volume=61 \| issue=1 \| title=Interactions of macromolecules with salt ions: an electrostatic theory for the Hofmeister effect \|date=October 2005 \| pages=69–78 \| last1 = Zhou \| first1 = Huan-Xiang \| journal = Proteins: Structure, Function, and Bioinformatics}}
			* Tanford C and Reynolds J. (2001) ''Nature's robots: a history of proteins'', Oxford University Press. ISBN 0-19-850466-7
			* Creighton TE. (1993) ''Proteins'', 2nd ed., W. H. Freeman. ISBN 0-7167-2317-4
			* Jencks WP. (1969) ''Catalysis in Chemistry and Enzymology'', Dover republication (1987). ISBN 0-486-65460-5
			* {{cite journal \| last1 = Collins \| first1 = KD. \| last2 = Washabaugh \| first2 = MW. \| year = 1985 \| title = The Hofmeister effect and the behaviour of water at interfaces \| url = \| journal = Q Rev Biophys \| volume = 18 \| issue = 4\| pmid = 3916340 \| pages = 323–422 }}

			{{See also\|Hofmeister (disambiguation){{!}}Hofmeister}}

			{{Persondata <!-- Metadata: see [[Wikipedia:Persondata]]. -->
			\| NAME = Hofmeister, Franz
			\| ALTERNATIVE NAMES =
			\| SHORT DESCRIPTION = German scientist
			\| DATE OF BIRTH = 1850
			\| PLACE OF BIRTH = [[Prague]]
			\| DATE OF DEATH = 1922
			\| PLACE OF DEATH =
			}}
			{{DEFAULTSORT:Hofmeister, Franz}}
			[[Category:1850 births]]
			[[Category:1922 deaths]]
			[[Category:19th-century German people]]
			[[Category:20th-century German people]]
			[[Category:19th-century Czech people]]
			[[Category:19th-century chemists]]
			[[Category:20th-century chemists]]
			[[Category:German chemists]]
			[[Category:Czech chemists]]
			[[Category:German biochemists]]
			[[Category:German people of German Bohemian descent]]
			[[Category:German Bohemian people]]
			[[Category:People from Prague]]

en>Srleffler: dab loading

2012-07-15T19:48:46Z

dab loading

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