東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Application of the solute partitioni...

Pegram, Laurel M.

FindBook

Google Book

Amazon

博客來

Application of the solute partitioning model to quantify Hofmeister ion effects on model processes and protein folding.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Application of the solute partitioning model to quantify Hofmeister ion effects on model processes and protein folding./
作者:	Pegram, Laurel M.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2007,
面頁冊數:	112 p.
附註:	Source: Dissertation Abstracts International, Volume: 68-12, Section: B, page: 8052.
Contained By:	Dissertation Abstracts International68-12B.
標題:	Physical chemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3294131
ISBN:	9780549379355

Application of the solute partitioning model to quantify Hofmeister ion effects on model processes and protein folding.
Pegram, Laurel M.

Application of the solute partitioning model to quantify Hofmeister ion effects on model processes and protein folding. - Ann Arbor : ProQuest Dissertations & Theses, 2007 - 112 p.

Source: Dissertation Abstracts International, Volume: 68-12, Section: B, page: 8052.

Thesis (Ph.D.)--The University of Wisconsin - Madison, 2007.

Quantitative interpretation and prediction of Hofmeister salt effects on protein processes, including folding and crystallization, have been elusive goals of a century of research. We have developed a surface-bulk ion partitioning model, analogous to a model developed previously for the interpretation of solute effects on biopolymer processes, and applied it to analyze literature surface tension data for aqueous salt solutions. Single-ion partition coefficients are found to be independent of bulk salt concentration and additive for different salt ions. These partition coefficients provide a quantitative means of comparison with surface-sensitive spectroscopic measurements and with predictions of molecular dynamics simulations. In most cases, rank orders of partition coefficients for the air-water surface follow the conventional biopolymer Hofmeister series, but cations are shifted (toward exclusion) as compared with inferred values for interactions with protein surface.

ISBN: 9780549379355Subjects--Topical Terms:

1981412
Physical chemistry.

Application of the solute partitioning model to quantify Hofmeister ion effects on model processes and protein folding.
LDR:03533nmm a2200325 4500 001 2164197
005 20181030085012.5
008 190424s2007 ||||||||||||||||| ||eng d
020 $a 9780549379355
035 $a (MiAaPQ)AAI3294131
035 $a AAI3294131
040 $a MiAaPQ $c MiAaPQ
100 1 $a Pegram, Laurel M. $3 3352242
245 1 0 $a Application of the solute partitioning model to quantify Hofmeister ion effects on model processes and protein folding.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2007
300 $a 112 p.
500 $a Source: Dissertation Abstracts International, Volume: 68-12, Section: B, page: 8052.
500 $a Adviser: M. Thomas Record, Jr.
502 $a Thesis (Ph.D.)--The University of Wisconsin - Madison, 2007.
520 $a Quantitative interpretation and prediction of Hofmeister salt effects on protein processes, including folding and crystallization, have been elusive goals of a century of research. We have developed a surface-bulk ion partitioning model, analogous to a model developed previously for the interpretation of solute effects on biopolymer processes, and applied it to analyze literature surface tension data for aqueous salt solutions. Single-ion partition coefficients are found to be independent of bulk salt concentration and additive for different salt ions. These partition coefficients provide a quantitative means of comparison with surface-sensitive spectroscopic measurements and with predictions of molecular dynamics simulations. In most cases, rank orders of partition coefficients for the air-water surface follow the conventional biopolymer Hofmeister series, but cations are shifted (toward exclusion) as compared with inferred values for interactions with protein surface.
520 $a The SPM is then applied to literature solubility/distribution data for hydrocarbons and model peptides. Both the hydration layer thickness and rank orders of anion and cation interactions with hydrocarbon surface are similar to those calculated for the air-water surface. Application of a course-grained surface area decomposition (e.g., nonpolar, polar amide) to the model peptide data allows determination of partition coefficients for amide surface. All salts investigated are found to accumulate at amide surface to a similar extent. Ion effects are independent and additive, allowing successful prediction of salt effects on model micelle formation and peptide solubility.
520 $a From the model compound analysis, we propose that the spectrum of Hofmeister salt effects observed for protein unfolding is due to the large amounts of nonpolar (hydrocarbon) surface exposed in this process. Salts that are only weakly excluded from nonpolar surface (e.g. GuHCl) are denturants because of their accumulation at amide surface. Since the vast majority of the surface exposed in unfolding is nonpolar or polar amide, we test the model compound predictions by applying the SPM to the thermodynamics of unfolding a small globular protein, monitored by circular dichroism spectroscopy. A preliminary separation of Coulombic and Hofmeister effects allows determination of Hofmeister interaction coefficients which are in good agreement with those predicted from the model compound analysis and coarse-grained DeltaASA decomposition.
590 $a School code: 0262.
650 4 $a Physical chemistry. $3 1981412
650 4 $a Biochemistry. $3 518028
650 4 $a Biophysics. $3 518360
690 $a 0494
690 $a 0487
690 $a 0786
710 2 $a The University of Wisconsin - Madison. $3 626640
773 0 $t Dissertation Abstracts International $g 68-12B.
790 $a 0262
791 $a Ph.D.
792 $a 2007
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3294131