Enhanced thermostability of methyl parathion hydrolase from Ochrobactrum sp. M231 by rational engineering of a glycine to proline mutation

J Tian, P Wang, S Gao, X Chu, N Wu, Y Fan - The FEBS journal, 2010 - Wiley Online Library
Protein thermostability can be increased by some glycine to proline mutations in a target
protein. However, not all glycine to proline mutations can improve protein thermostability …

[HTML][HTML] Dinâmica molecular: teoria e aplicações em planejamento de fármacos

AM Namba, VB da Silva, C Da Silva - Eclética Química, 2008 - SciELO Brasil
Dinâmica Molecular (DM) é uma ferramenta computacional poderosa usada em Química
Medicinal para o planejamento racional de fármacos. DM é uma extensão da Mecânica …

Improvement of the acid resistance, catalytic efficiency, and thermostability of nattokinase by multisite‐directed mutagenesis

Z Liu, H Zhao, L Han, W Cui, L Zhou… - Biotechnology and …, 2019 - Wiley Online Library
Nattokinase (NK) is a serine protease of the subtilisin family; as a potent fibrinolytic enzyme,
it is potentially useful for thrombosis therapy. For NK to be applied as an oral medicine for …

Binding of Anionic Polyacrylamide with Amidase and Laccase under 298, 303, and 308 K: Docking and Molecular Dynamics Simulation Studies Combined with …

F Wang, L Zhang, D Zhang, X Wu, S Deng - ACS omega, 2023 - ACS Publications
Amidase and laccase play a key role in the degradation process of anionic polyacrylamide
(HPAM). However, the largest challenge of HPAM enzymatic degradation is whether the …

Enhanced Thermal Stability and Hydrolytic Ability of Bacillus subtilis Aminopeptidase by Removing the Thermal Sensitive Domain in the Non-Catalytic Region

X Gao, Z Liu, W Cui, L Zhou, Y Tian, Z Zhou - PLoS One, 2014 - journals.plos.org
Besides the catalytic ability, many enzymes contain conserved domains to perform some
other physiological functions. However, sometimes these conserved domains were …

The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors

AF Noel, O Bilsel, A Kundu, Y Wu, JA Zitzewitz… - Journal of molecular …, 2009 - Elsevier
Spontaneous mutations at numerous sites distant from the active site of human
immunodeficiency virus type 1 protease enable resistance to inhibitors while retaining …

Modification of nitrile hydratase from Rhodococcus erythropolis CCM2595 by semirational design to enhance its substrate affinity

L Wang, B Cui, K Qiu, J Huang, C Liang - Biointerphases, 2022 - pubs.aip.org
Nitrile hydratase (NHase, EC 4.2. 1.84) is an excellent biocatalyst that catalyzes the
hydration of nitrile substances to their corresponding amides. Given its catalytic specificity …

Visualization of early events in acetic acid denaturation of HIV-1 protease: a molecular dynamics study

AN Borkar, MK Rout, RV Hosur - PLoS One, 2011 - journals.plos.org
Protein denaturation plays a crucial role in cellular processes. In this study, denaturation of
HIV-1 Protease (PR) was investigated by all-atom MD simulations in explicit solvent. The PR …

[PDF][PDF] Multiple routes and milestones in the folding of HIV-1 protease monomer

M Bonomi, A Barducci, FL Gervasio, M Parrinello - Biophysical Journal, 2010 - cell.com
Evolution has lead proteins to display funneled energy landscapes with small degrees of
ruggedness. However, a funneled landscape does not preclude the presence of multiple …

[PDF][PDF] Atomistic simulations of the HIV-1 protease folding inhibition

G Verkhivker, G Tiana, C Camilloni, D Provasi… - Biophysical journal, 2008 - cell.com
Biochemical experiments have recently revealed that the p-S8 peptide, with an amino-acid
sequence identical to the conserved fragment 83–93 (S8) of the HIV-1 protease, can inhibit …