The nature of enzyme catalysis in trypsin.

The nature of enzyme catalysis in trypsin.

Item
http://www.wikidata.org/entity/Q35588282
Enzymes work by solvation substitution rather than by desolvation.On achieving better than 1-A accuracy in a simulation of a large protein: Streptomyces griseus protease ATheoretical studies on the dihydrofolate reductase mechanism: electronic polarization of bound substrates.Improved Production of Active Streptomyces griseus Trypsin with a Novel Auto-Catalyzed StrategyProtein engineering. The design, synthesis and characterization of factitious proteins.Effect of specificity on ligand conformation in acyl-chymotrypsinsHydrogen-bonding in enzyme catalysis. Fourier-transform infrared detection of ground-state electronic strain in acyl-chymotrypsins and analysis of the kinetic consequences.Simulations of dynamical properties of a Michaelis complex: porcine pancreatic elastase and the hexapeptide, Thr-Pro-n Val-Leu-Tyr-Thr.Catalysis by solvation rather than the desolvation effect: exploring the catalytic efficiency of SAM-dependent chlorinase.Roles of electrostatic interaction in proteins.
P2860

The nature of enzyme catalysis in trypsin.

Item
http://www.wikidata.org/entity/Q35588282
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
The nature of enzyme catalysis in trypsin.
@ast
The nature of enzyme catalysis in trypsin.
@en
type
label
The nature of enzyme catalysis in trypsin.
@ast
The nature of enzyme catalysis in trypsin.
@en
prefLabel
The nature of enzyme catalysis in trypsin.
@ast
The nature of enzyme catalysis in trypsin.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
The nature of enzyme catalysis in trypsin.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932