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

FindBook

Google Book

Amazon

博客來

Pressure Adaptations in Deep-Sea Dihydrofolate Reductases.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Pressure Adaptations in Deep-Sea Dihydrofolate Reductases./
作者:	Penhallurick, Ryan W.
面頁冊數:	1 online resource (204 pages)
附註:	Source: Dissertations Abstracts International, Volume: 83-11, Section: B.
Contained By:	Dissertations Abstracts International83-11B.
標題:	Biophysics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=29165139click for full text (PQDT)
ISBN:	9798426835849

Pressure Adaptations in Deep-Sea Dihydrofolate Reductases.
Penhallurick, Ryan W.

Pressure Adaptations in Deep-Sea Dihydrofolate Reductases. - 1 online resource (204 pages)

Source: Dissertations Abstracts International, Volume: 83-11, Section: B.

Thesis (Ph.D.)--Georgetown University, 2022.

Includes bibliographical references

Deep-sea organisms must have proteins that function under high hydrostatic pressure to survive. Adaptations used in proteins from "pressure-loving" piezophiles may include greater compressibility or greater stability against pressure-induced destabilization. Here, adaptations to temperature and pressure in the ubiquitous enzyme dihydrofolate reductase from several deep-sea microbes are examined with molecular dynamics computer simulations and high pressure small angle neutron and X-ray scattering. A mechanism of how addition of a single methylene from Asp27 in DHFR of the piezosensitive mesophile E. coli to Glu27, which was originally identified in a DHFR from a moderate piezophile M. profunda, may alleviate improper overcorrelated motions at compressive pressures is discussed, along with experimental comparisons of pressure effects on these enzymes. Enhanced stability and a mechanism for prevention of internal cavity solvation under significantly elevated pressure in DHFR from a hyperpiezophile isolated from the Marianas Trench is also proposed. This work aims to provide insight into pressure adaptations employed in various deep-sea dihydrofolate reductases to expand on how enzymes from piezophiles balance flexibility and stability to maintain proper functioning at elevated pressure.

Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2023

Mode of access: World Wide Web

ISBN: 9798426835849Subjects--Topical Terms:

518360
Biophysics.
Subjects--Index Terms:

Deep-sea adaptationsIndex Terms--Genre/Form:

542853
Electronic books.

Pressure Adaptations in Deep-Sea Dihydrofolate Reductases.
LDR:02733nmm a2200421K 4500 001 2354852
005 20230505090440.5
006 m o d
007 cr mn ---uuuuu
008 241011s2022 xx obm 000 0 eng d
020 $a 9798426835849
035 $a (MiAaPQ)AAI29165139
035 $a AAI29165139
040 $a MiAaPQ $b eng $c MiAaPQ $d NTU
100 1 $a Penhallurick, Ryan W. $3 3695226
245 1 0 $a Pressure Adaptations in Deep-Sea Dihydrofolate Reductases.
264 0 $c 2022
300 $a 1 online resource (204 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: Dissertations Abstracts International, Volume: 83-11, Section: B.
500 $a Advisor: Ichiye, Toshiko.
502 $a Thesis (Ph.D.)--Georgetown University, 2022.
504 $a Includes bibliographical references
520 $a Deep-sea organisms must have proteins that function under high hydrostatic pressure to survive. Adaptations used in proteins from "pressure-loving" piezophiles may include greater compressibility or greater stability against pressure-induced destabilization. Here, adaptations to temperature and pressure in the ubiquitous enzyme dihydrofolate reductase from several deep-sea microbes are examined with molecular dynamics computer simulations and high pressure small angle neutron and X-ray scattering. A mechanism of how addition of a single methylene from Asp27 in DHFR of the piezosensitive mesophile E. coli to Glu27, which was originally identified in a DHFR from a moderate piezophile M. profunda, may alleviate improper overcorrelated motions at compressive pressures is discussed, along with experimental comparisons of pressure effects on these enzymes. Enhanced stability and a mechanism for prevention of internal cavity solvation under significantly elevated pressure in DHFR from a hyperpiezophile isolated from the Marianas Trench is also proposed. This work aims to provide insight into pressure adaptations employed in various deep-sea dihydrofolate reductases to expand on how enzymes from piezophiles balance flexibility and stability to maintain proper functioning at elevated pressure.
533 $a Electronic reproduction. $b Ann Arbor, Mich. : $c ProQuest, $d 2023
538 $a Mode of access: World Wide Web
650 4 $a Biophysics. $3 518360
650 4 $a Microbiology. $3 536250
650 4 $a Biochemistry. $3 518028
650 4 $a Biological oceanography. $3 2122748
653 $a Deep-sea adaptations
653 $a Dihydrofolate reductase
653 $a Molecular dynamics simulations
653 $a Piezophiles
653 $a Pressure
653 $a Small-angle scattering
655 7 $a Electronic books. $2 lcsh $3 542853
690 $a 0786
690 $a 0487
690 $a 0410
690 $a 0416
710 2 $a ProQuest Information and Learning Co. $3 783688
710 2 $a Georgetown University. $b Chemistry. $3 1064523
773 0 $t Dissertations Abstracts International $g 83-11B.
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=29165139 $z click for full text (PQDT)