Role of active site rigidity in activity: MD simulation and fluorescence study on a lipase mutant.
about
Structural Rigidity and Protein Thermostability in Variants of Lipase A from Bacillus subtilisThermostability of in vitro evolved Bacillus subtilis lipase A: a network and dynamics perspective.Dynamically-driven enhancement of the catalytic machinery of the SARS 3C-like protease by the S284-T285-I286/A mutations on the extra domain.Computational library design for increasing haloalkane dehalogenase stability.Molecular dynamics study of naturally existing cavity couplings in proteins.Improving the Thermostability and Activity of a Thermophilic Subtilase by Incorporating Structural Elements of Its Psychrophilic Counterpart.Bacterial toxin RelE: a highly efficient ribonuclease with exquisite substrate specificity using atypical catalytic residuesCutoff lensing: predicting catalytic sites in enzymes.Interactions of oximino-substituted boronic acids and β-lactams with the CMY-2-derived extended-spectrum cephalosporinases CMY-30 and CMY-42Lipase in aqueous-polar organic solvents: activity, structure, and stability.Increasing the stability of the bacteriophage endolysin PlyC using rationale-based FoldX computational modeling.The Role of Solvent-Accessible Leu-208 of Cold-Active Pseudomonas fluorescens Strain AMS8 Lipase in Interfacial Activation, Substrate Accessibility and Low-Molecular Weight Esterification in the Presence of Toluene.The Effect of N-Terminal Domain Removal towards the Biochemical and Structural Features of a Thermotolerant Lipase from an Antarctic Pseudomonas sp. Strain AMS3.Proline substitutions in a Mip-like peptidyl-prolyl cis-trans isomerase severely affect its structure, stability, shape and activity.
P2860
Q27304404-478D5F0C-31CC-4D42-BA4E-C2758A243BBCQ30365682-FC019636-FE2C-4732-B358-068B1FD4760DQ33921124-68341F2D-6D59-40C0-AAFB-DCAABA2014C3Q35197299-EE0E1785-F4C4-4622-90EB-BC1808ACBB8EQ35588863-B33D380A-C2A3-4181-A177-58E5610AFBB8Q35973150-903B1C6E-C041-4963-98B7-760CC1E57D2EQ37542065-A5A6CE92-96BC-4A63-AB6D-5CF76390637DQ41140874-47BD0B72-3276-405A-A657-315DA7854B7DQ41821008-40260CD7-C2DC-4758-9C5A-02F6BE89EAEFQ41971027-834D04DD-5C4D-47F7-84D2-5532CF45A72CQ42157372-7400C13B-AC55-47F0-A514-9091AF52C3D1Q47194400-30760E82-E2A4-461D-A803-889186F48098Q50042167-B3BD7D36-35DD-46DE-BFF7-CBF8814F2C78Q54264024-49D9FA19-18C6-4FBA-B9E8-E550297B2231
P2860
Role of active site rigidity in activity: MD simulation and fluorescence study on a lipase mutant.
description
2012 nî lūn-bûn
@nan
2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
name
Role of active site rigidity i ...... ence study on a lipase mutant.
@ast
Role of active site rigidity i ...... ence study on a lipase mutant.
@en
Role of active site rigidity i ...... ence study on a lipase mutant.
@nl
type
label
Role of active site rigidity i ...... ence study on a lipase mutant.
@ast
Role of active site rigidity i ...... ence study on a lipase mutant.
@en
Role of active site rigidity i ...... ence study on a lipase mutant.
@nl
prefLabel
Role of active site rigidity i ...... ence study on a lipase mutant.
@ast
Role of active site rigidity i ...... ence study on a lipase mutant.
@en
Role of active site rigidity i ...... ence study on a lipase mutant.
@nl
P2093
P2860
P1433
P1476
Role of active site rigidity i ...... ence study on a lipase mutant.
@en
P2093
G Krishnamoorthy
Md Zahid Kamal
Nalam Madhusudhana Rao
P2860
P304
P356
10.1371/JOURNAL.PONE.0035188
P407
P577
2012-04-13T00:00:00Z