منابع مشابه
Facilitated diffusion during catalysis by EcoRI endonuclease. Nonspecific interactions in EcoRI catalysis.
The potential for processive EcoRI endonuclease hydrolysis has been examined on several DNA substrates containing two EcoRI sites which were embedded in identical sequence environments. With a 388-base pair circular DNA, in which the two recognition sites are separated by 51 base pairs (shorter distance) or 337 base pairs (longer distance), 77 and 34% of all events involved processive hydrolysi...
متن کاملContribution of cation-π interactions in iminium catalysis.
Ab initio calculations were carried out for a benzyl-substituted iminium cation derived from (E)-crotonaldehyde and a chiral imidazolidinone that was developed as an organocatalyst by MacMillan et al. At the MP2 level of theory it is predicted that the phenyl group is close to the iminium moiety in the most stable conformer, suggesting that the cation-π interaction contributes to the stabilizat...
متن کاملRole of Charge-transfer Interactions in Flavoprotein Catalysis
The last decade has produced a veritable explosion of knowledge on the chemical reactivity of the isoalloxazine ring system of the flavin coenzymes, largely because of a side-by-side development with knowledge of flavoenzymes and model flavin studies. In this period the visible absorption spectra and epr spectra of the flavin semiquinone in its cationic, neutral, and anionic forms have been def...
متن کاملHeadgroup-Dependent Membrane Catalysis of Apelin−Receptor Interactions Is Likely
Apelin is the peptidic ligand for the G-protein-coupled receptor APJ. The apelin-APJ system is important in cardiovascular regulation, fluid homeostasis, and angiogenesis, among other roles. In this study, we investigate interactions between apelin and membrane-mimetic micelles of the detergents sodium dodecyl sulfate (SDS), dodecylphosphocholine (DPC), and 1-palmitoyl-2-hydroxy-sn-glycero-3-[p...
متن کاملLoop interactions during catalysis by dihydrofolate reductase from Moritella profunda.
Dihydrofolate reductase (DHFR) is often used as a model system to study the relation between protein dynamics and catalysis. We have studied a number of variants of the cold-adapted DHFR from Moritella profunda (MpDHFR), in which the catalytically important M20 and FG loops have been altered, and present a comparison with the corresponding variants of the well-studied DHFR from Escherichia coli...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Organic Chemistry
سال: 2020
ISSN: 1434-193X,1099-0690
DOI: 10.1002/ejoc.202000660