Atomic Scale Determination of Enzyme Flexibility and Active Site Stability through Static Modes: Case of Dihydrofolate Reductase

2011 ◽  
Vol 115 (7) ◽  
pp. 1616-1622 ◽  
Author(s):  
Marie Brut ◽  
Alain Estève ◽  
Georges Landa ◽  
Guillaume Renvez ◽  
Mehdi Djafari Rouhani ◽  
...  
Keyword(s):  
Dihydrofolate Reductase ◽  
Active Site ◽  
Atomic Scale

Statistical Description of Isotope Exchange Processes: A Multisite Model for the 18O Exchange

1982 ◽  
Vol 37 (11-12) ◽  
pp. 1161-1169 ◽  
Author(s):  
Paul Rösch
Keyword(s):  
Active Site ◽  
Isotope Exchange ◽  
Analytical Procedure ◽  
Matrix Formalism ◽  
Model Calculations ◽  
Exchange Processes ◽  
Reaction Solution ◽  
Different Types ◽  
Refinement Procedure

Abstract An analytical procedure has been developed for the determination of isotope exchange processes as exemplified by the 18O exchange catalysed by enzyme-nucleotide complexes. The model is able to handle more than one type of active site per reaction solution and is also able to distinguish between different types of inequivalence of the oxygens of enzyme bound Pi. Use of transition matrix formalism and basic statistical considerations lead directly to the simple model. A data refinement procedure is introduced and model calculations are shown.

Nonlinear Vibrations in a 2-Dimensional Protein Cluster Model with Linear Bonds

2000 ◽  
Vol 214 (1) ◽  
Author(s):  
E.G. Shidlovskaya ◽  
L. Schimansky-Geier ◽  
Yu.M. Romanovsky
Keyword(s):  
Active Site ◽  
Internal Resonance ◽  
Cluster Model ◽  
Active Sites ◽  
Nonlinear Vibrations ◽  
Nonlinear Phenomena ◽  
Two Dimensional ◽  
Dimensional Model ◽  
Two Dimensional Model

A two dimensional model for the substrate inside a pocket of an active site of an enzyme is presented and investigated as a vibrational system. The parameters of the system are evaluated for α-chymotrypsin. In the case of internal resonance it is analytically and numerically shown that the energy concentrated on a certain degree of freedom might be several times larger than in the non-resonant case. Additionally, the system is driven by harmonic excitations and again energy due to nonlinear phenomena is redistributed inhomogeneously. These results may be of importance for the determination of the rates of catalytic events of substrates bound in pockets of active sites.

scholarly journals Inside Cover: Atomic-Scale Determination of Active Facets on the MoVTeNb Oxide M1 Phase and Their Intrinsic Catalytic Activity for Ethane Oxidative Dehydrogenation (Angew. Chem. Int. Ed. 31/2016)

2016 ◽  
Vol 55 (31) ◽  
pp. 8770-8770
Author(s):  
Daniel Melzer ◽  
Pinghong Xu ◽  
Daniela Hartmann ◽  
Yuanyuan Zhu ◽  
Nigel D. Browning ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Oxidative Dehydrogenation ◽  
Atomic Scale ◽  
M1 Phase ◽  
Ethane Oxidative Dehydrogenation

Potentiometric determination of ionizations at the active site of papain

Biochemistry ◽  
1976 ◽  
Vol 15 (23) ◽  
pp. 5009-5017 ◽  
Author(s):  
Sidney D. Lewis ◽  
Frederick A. Johnson ◽  
Jules A. Shafer
Keyword(s):  
Active Site ◽  
Potentiometric Determination

Independent 5' and 3'-end determination of multiple dihydrofolate reductase transcripts

1987 ◽  
Vol 7 (10) ◽  
pp. 3732-3739
Author(s):  
J Y Yen ◽  
R E Kellems
Keyword(s):  
Dihydrofolate Reductase ◽  
Relative Abundance ◽  
Transcription Initiation ◽  
Promoter Region ◽  
Overlapping Genes ◽  
Cytoplasmic Rna ◽  
Upstream Promoter ◽  
Upstream Promoter Region ◽  
Polyadenylation Sites

Multiple dihydrofolate reductase (dhfr) mRNAs, differing substantially in abundance, are produced as a result of the utilization of multiple transcription initiation sites and multiple polyadenylation sites. We have shown that dhfr mRNAs initiating from an upstream promoter region utilize the same collection of six polyadenylation sites and generate multiple dhfr mRNAs at the same relative abundance as do the mRNAs initiating from the major transcription promoter region. These results indicate that the 5' and 3' ends of dhfr mRNAs are independently determined. We show that the relative abundance of steady-state dhfr mRNAs was the same in nuclear and cytoplasmic RNA fractions. This finding makes it unlikely that differences in mRNA stability account for differences in the relative abundance of the multiple dhfr mRNAs in the cytoplasm. Our analysis of the dhfr promoter region revealed the existence of stable cytoplasmic polyadenylated transcripts complementary to the first 300 nucleotides of the dhfr transcripts initiating from the upstream promoter region. Therefore, the dhfr locus hosts two divergent and partially overlapping genes which share the same promoter region.

Spectroscopic studies on plastocyanin single crystals: a detailed electronic structure determination of the blue copper active site

1981 ◽  
Vol 103 (15) ◽  
pp. 4382-4388 ◽  
Author(s):  
K. W. Penfield ◽  
R. R. Gay ◽  
R. S. Himmelwright ◽  
N. C. Eickman ◽  
V. A. Norris ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Single Crystals ◽  
Structure Determination ◽  
Active Site ◽  
Spectroscopic Studies ◽  
Blue Copper

scholarly journals Expression, Purification and Characterization of the Enzyme II Mannitol-Specific Domain from Staphylococcus carnosus and Determination of the Active-Site Cysteine Residue

1995 ◽  
Vol 233 (1) ◽  
pp. 116-122 ◽  
Author(s):  
Rembert Pogge Strandmann ◽  
Christiane Weigt ◽  
Roland Fischer ◽  
Helmut E. Meyer ◽  
Hans Robert Kalbitzer ◽  
...  
Keyword(s):  
Active Site ◽  
Cysteine Residue ◽  
Purification And Characterization ◽  
Specific Domain ◽  
Active Site Cysteine ◽  
Staphylococcus Carnosus ◽  
Active Site Cysteine Residue
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