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Chemical and biophysical approaches ...

Blankenship, John William.

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Chemical and biophysical approaches to understanding protein stability.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Chemical and biophysical approaches to understanding protein stability./
作者:	Blankenship, John William.
面頁冊數:	267 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0691.
Contained By:	Dissertation Abstracts International64-02B.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3081336

Chemical and biophysical approaches to understanding protein stability.
Blankenship, John William.

Chemical and biophysical approaches to understanding protein stability. - 267 p.

Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0691.

Thesis (Ph.D.)--The Scripps Research Institute, 2003.

Most functional proteins assume a specific three-dimensional structure, or a fold, which is key for the protein's activity and specificity. Many initial assumptions about protein function that assumed a static or rigid body have since been proven to be false in many cases—proteins can change conformation during the course of enzymatic catalysis, or use a change in stability to direct their activity. New techniques for protein engineering, coupled with biophysical analysis, enable us to characterize these dynamics as well as engineer them to alter the stability and activity of proteins. In this thesis, I will discuss four overall systems:Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Chemical and biophysical approaches to understanding protein stability.
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100 1 $a Blankenship, John William. $3 1944685
245 1 0 $a Chemical and biophysical approaches to understanding protein stability.
300 $a 267 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0691.
500 $a Adviser: Philip Dawson.
502 $a Thesis (Ph.D.)--The Scripps Research Institute, 2003.
520 $a Most functional proteins assume a specific three-dimensional structure, or a fold, which is key for the protein's activity and specificity. Many initial assumptions about protein function that assumed a static or rigid body have since been proven to be false in many cases—proteins can change conformation during the course of enzymatic catalysis, or use a change in stability to direct their activity. New techniques for protein engineering, coupled with biophysical analysis, enable us to characterize these dynamics as well as engineer them to alter the stability and activity of proteins. In this thesis, I will discuss four overall systems:
520 $a <italic>In chapter 1</italic>, I discuss NMR structural characterization of the <super>15</super>N-labeled N56A mutant of calbindin D<sub>9k</sub>, a calcium-binding protein with two EF-hand Ca<super>2+</super> binding domains that exhibits allostery between its two Ca<super>2+</super> binding sites (under Walter Chazin, and with Lena Maler). These structural studies elucidated the structure and dynamics of the remaining uncharacterized intermediate within the calcium binding cycle.
520 $a <italic>In chapter 2</italic>, I discuss attempts to engineer the active site of glutaredoxin 1 and 3 by solid phase peptide synthesis. Both are small disulfide oxidoreductases that are similar in sequence but use their fold to either stabilize or destabilize their active-site disulfide bond.
520 $a <italic>In chapter 3</italic>, I discuss probing the backbone hydrogen bonds within the unusually stable and well-packed hydrophobic core of the leucine zipper GCN4 (with Rema Balambika) by incorporating ester backbone substitutions. This study provided an estimate of the strength of those hydrogen bonds, as well as provided insight into the effect of amide to ester backbone substitutions.
520 $a <italic>In chapter 4</italic>, I discuss the design of an isolated protein with a single topological link, a protein [2]catenane. This alternative crosslink results in a notable increase in resistance to denaturation and proteolysis, while maintaining the protein fold.
520 $a <italic>In chapter 5</italic>, I discuss the design of a protein pseudorotaxane, a protein that can only fold by threading of a single linear chain through a second, cyclic chain. This model system should prove valuable for the study of protein:protein association and protein folding.
590 $a School code: 1179.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
650 4 $a Biology, Molecular. $3 1017719
690 $a 0487
690 $a 0786
690 $a 0307
710 2 0 $a The Scripps Research Institute. $3 1251203
773 0 $t Dissertation Abstracts International $g 64-02B.
790 1 0 $a Dawson, Philip, $e advisor
790 $a 1179
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3081336