國立虎尾科技大學 |

Hofmeister chemistry : = Weak cation binding to protein backbones & biomolecular size influence on specific ion effects.

Record Type:	Language materials, manuscript : Monograph/item
Title/Author:	Hofmeister chemistry :/
Reminder of title:	Weak cation binding to protein backbones & biomolecular size influence on specific ion effects.
Author:	Okur, Halil Ibrahim.
Description:	1 online resource (120 pages)
Notes:	Source: Dissertation Abstracts International, Volume: 78-04(E), Section: B.
Contained By:	Dissertation Abstracts International78-04B(E).
Subject:	Physical chemistry. -
Online resource:	click for full text (PQDT)
ISBN:	9781369404944

Hofmeister chemistry : = Weak cation binding to protein backbones & biomolecular size influence on specific ion effects.
Okur, Halil Ibrahim.

Hofmeister chemistry :Weak cation binding to protein backbones & biomolecular size influence on specific ion effects. - 1 online resource (120 pages)

Source: Dissertation Abstracts International, Volume: 78-04(E), Section: B.

Thesis (Ph.D.)--The Pennsylvania State University, 2014.

Includes bibliographical references

The behavior of solutes in aqueous solutions was first shown over a century ago to be ion specific. Such ion specificity has been characterized and named as the lyotropic or Hofmeister series. These recurring ion trends have been elucidated for a wide range of biologically important processes including aggregation of polymers/proteins, protein folding, and enzymatic activities. In this dissertation, we investigated two major issues yet to be solved in ion specific effects on biomacromolecular systems. First, cation associations to the protein backbone was investigated with three different model systems. A simple amide molecule, butyramide, was utilized as a monomer unit for protein backbone. FTIR spectroscopy is employed to monitor the amide I band, and coupled with vibrational sum frequency spectroscopy (VSFS), which shows aligned water hydration at the air/butyramide/water interface. Contact paired cation binding is monitored via a salt concentration dependent new carbonyl stretch peak (1645 cm-1), which is &sim;25 cm -1 blue shifted from the original resonance (1620 cm-1). Moreover, enhancement in the degree of aligned water molecules upon cation absorption in the hydration of the butyramide monolayer at the air/water interface demonstrated a complementary set of evidence. Only strongly hydrated cations (Mg2+, Ca2+, Li+) demonstrated these spectral changes. Weakly hydrated cations (Na+, K +), on the other hand, did not show any evidence for contact paired binding to simple amides.

Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2018

Mode of access: World Wide Web

ISBN: 9781369404944Subjects--Topical Terms:

1148725
Physical chemistry.
Index Terms--Genre/Form:

554714
Electronic books.

Hofmeister chemistry : = Weak cation binding to protein backbones & biomolecular size influence on specific ion effects.
LDR:04926ntm a2200349Ki 4500 001 918635
005 20181030085011.5
006 m o u
007 cr mn||||a|a||
008 190606s2014 xx obm 000 0 eng d
020 $a 9781369404944
035 $a (MiAaPQ)AAI10297081
035 $a AAI10297081
040 $a MiAaPQ $b eng $c MiAaPQ $d NTU
100 1 $a Okur, Halil Ibrahim. $3 1193007
245 1 0 $a Hofmeister chemistry : $b Weak cation binding to protein backbones & biomolecular size influence on specific ion effects.
264 0 $c 2014
300 $a 1 online resource (120 pages)
336 $a text $b txt $2 rdacontent
337 $a computer $b c $2 rdamedia
338 $a online resource $b cr $2 rdacarrier
500 $a Source: Dissertation Abstracts International, Volume: 78-04(E), Section: B.
500 $a Adviser: Paul S. Cremer.
502 $a Thesis (Ph.D.)--The Pennsylvania State University, 2014.
504 $a Includes bibliographical references
520 $a The behavior of solutes in aqueous solutions was first shown over a century ago to be ion specific. Such ion specificity has been characterized and named as the lyotropic or Hofmeister series. These recurring ion trends have been elucidated for a wide range of biologically important processes including aggregation of polymers/proteins, protein folding, and enzymatic activities. In this dissertation, we investigated two major issues yet to be solved in ion specific effects on biomacromolecular systems. First, cation associations to the protein backbone was investigated with three different model systems. A simple amide molecule, butyramide, was utilized as a monomer unit for protein backbone. FTIR spectroscopy is employed to monitor the amide I band, and coupled with vibrational sum frequency spectroscopy (VSFS), which shows aligned water hydration at the air/butyramide/water interface. Contact paired cation binding is monitored via a salt concentration dependent new carbonyl stretch peak (1645 cm-1), which is &sim;25 cm -1 blue shifted from the original resonance (1620 cm-1). Moreover, enhancement in the degree of aligned water molecules upon cation absorption in the hydration of the butyramide monolayer at the air/water interface demonstrated a complementary set of evidence. Only strongly hydrated cations (Mg2+, Ca2+, Li+) demonstrated these spectral changes. Weakly hydrated cations (Na+, K +), on the other hand, did not show any evidence for contact paired binding to simple amides.
520 $a The molecular mechanism of cation-protein backbone interactions was further investigated on neutral biomacromolecules. The hydrophobic collapse of poly (N-isopropyl acrylamide) (PNIPAM) and elastin like polypeptides (ELPs) was exploited to glean the effect of 11 alkali and alkaline earth metal chloride salt. The lower critical solution temperature (LCST) data was modeled to a simple equation where weakly hydrated cations once again show no clue for cation binding to neutral biomolecules. These cations mainly salt macromolecules out with surface tension effects. Very weak cation binding, however, was shown for strongly hydrated cations. Moreover, an additional bulk salting-in effect was shown for strongly hydrated cations, where ion hydration thermodynamics demonstrated a direct correlation with the specific salting in effects.
520 $a The second major topic focused in this thesis was the molecular size influence on specific ion effects. It was investigated by using various poly( N,N diethyl acrylamide) (PDEA) from oligomers to large polymers, along with some simple amide molecules; N-methyl acetamide (NMA), and N,N Diethyl acetamide. Hydrophobic collapse of PDEA was probed as a function of three representative Hofmeister anions (SO 42-, Cl-, SCN-). Molecular size changes showed no apparent influence with kosmotropic SO4 2-, and Cl- anions. Nevertheless, chaotropic, SCN -, anion binding was dramatically influenced from molecular size. Similar results were achieved from the Raman spectrum of the model systems where the shifts in the C-H stretch peaks were monitored. Overall, weakly hydrated anion exclusion (KD > 3M), and a strong anion binding (KD &sim; 130mM) were observed for simple amides and large polymers, respectively. The molecular size dependence was also elucidated for the hydration of biomolecules. A gradual increase in the ice-like (3200 cm-1) water peak, which is attributed to weakly hydrated sites at the biomolecular surface, was monitored as the macromolecular size increases. This hydration behavior must play a dominant role for the underlying molecular mechanism for the macromolecular size effect.
533 $a Electronic reproduction. $b Ann Arbor, Mich. : $c ProQuest, $d 2018
538 $a Mode of access: World Wide Web
650 4 $a Physical chemistry. $3 1148725
650 4 $a Biochemistry. $3 582831
655 7 $a Electronic books. $2 local $3 554714
690 $a 0494
690 $a 0487
710 2 $a ProQuest Information and Learning Co. $3 1178819
710 2 $a The Pennsylvania State University. $3 845556
773 0 $t Dissertation Abstracts International $g 78-04B(E).
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10297081 $z click for full text (PQDT)