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Computer simulation of point mutatio...

Kani, Kian.

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Computer simulation of point mutations in carbonmonoxy myoglobin.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Computer simulation of point mutations in carbonmonoxy myoglobin./
Author:	Kani, Kian.
Description:	128 p.
Notes:	Source: Masters Abstracts International, Volume: 40-06, page: 1522.
Contained By:	Masters Abstracts International40-06.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1408837
ISBN:	0493622721

Computer simulation of point mutations in carbonmonoxy myoglobin.
Kani, Kian.

Computer simulation of point mutations in carbonmonoxy myoglobin. - 128 p.

Source: Masters Abstracts International, Volume: 40-06, page: 1522.

Thesis (M.S.)--California State University, Long Beach, 2002.

Based on published experimental data, an increase in binding affinity (−2.2 kcal/mol) exists for myoglobin (Mb) and carbon monoxide (CO) ligand when leucine occupies the 64<super>th</super> position (H64L) instead of wild type histidine. Molecular dynamics calculation of both wild type and H64L carbonmonoxy Mb were carried out at 300 K with explicit water solvent using the AMBER suite of programs. Estimates of the free energy difference between the two myoglobins was formed as the difference in energy as calculated by molecular dynamics. The resulting force field trajectories show the CO complex of H64L mutant to be 4.1 ± 0.8 kcal/mole less stable that the wild type.

ISBN: 0493622721Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Computer simulation of point mutations in carbonmonoxy myoglobin.
LDR:01482nam 2200265 a 45 001 935386
005 20110509
008 110509s2002 eng d
020 $a 0493622721
035 $a (UnM)AAI1408837
035 $a AAI1408837
040 $a UnM $c UnM
100 1 $a Kani, Kian. $3 1259075
245 1 0 $a Computer simulation of point mutations in carbonmonoxy myoglobin.
300 $a 128 p.
500 $a Source: Masters Abstracts International, Volume: 40-06, page: 1522.
502 $a Thesis (M.S.)--California State University, Long Beach, 2002.
520 $a Based on published experimental data, an increase in binding affinity (−2.2 kcal/mol) exists for myoglobin (Mb) and carbon monoxide (CO) ligand when leucine occupies the 64<super>th</super> position (H64L) instead of wild type histidine. Molecular dynamics calculation of both wild type and H64L carbonmonoxy Mb were carried out at 300 K with explicit water solvent using the AMBER suite of programs. Estimates of the free energy difference between the two myoglobins was formed as the difference in energy as calculated by molecular dynamics. The resulting force field trajectories show the CO complex of H64L mutant to be 4.1 ± 0.8 kcal/mole less stable that the wild type.
590 $a School code: 6080.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Chemistry, Inorganic. $3 517253
650 4 $a Computer Science. $3 626642
690 $a 0487
690 $a 0488
690 $a 0984
710 2 0 $a California State University, Long Beach. $3 1017843
773 0 $t Masters Abstracts International $g 40-06.
790 $a 6080
791 $a M.S.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1408837