𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Exploring the Drug-Binding Site Sudlow I of Human Serum Albumin: The Role of Water and Trp214 in Molecular Recognition and Ligand Binding

✍ Scribed by Dr. Osama K. Abou-Zied; Najla Al-Lawatia


Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
492 KB
Volume
12
Category
Article
ISSN
1439-4235

No coin nor oath required. For personal study only.


πŸ“œ SIMILAR VOLUMES


The role of configuration and conformati
✍ Julia Visy; MiklΓ³s Simonyi πŸ“‚ Article πŸ“… 1989 πŸ› John Wiley and Sons 🌐 English βš– 418 KB πŸ‘ 1 views

2,3-Benzodiazepines containing a centre of asymmetry at C-5 possess both central and helical chiralities, and the solution of their racemates contains four molecular species. The binding of these compounds to human serum albumin (HSA) was studied by affinity chromatography. The binding strength depe

Site I on human albumin: Differences in
✍ Carlo Bertucci; Alessandra Canepa; Giorgio A. Ascoli; Luis F. Lopes Guimaraes; G πŸ“‚ Article πŸ“… 1999 πŸ› John Wiley and Sons 🌐 English βš– 129 KB

The binding of drugs known to interact with area I on human serum albumin (HSA) was investigated using a chiral stationary phase obtained by anchoring HSA to a silica matrix. In particular, this high-pressure affinity chromatography selector was employed to study the binding properties of the indivi

Macromolecularization of a tripeptide an
✍ L. Michielin; S. Mammi; E. Peggion πŸ“‚ Article πŸ“… 1983 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 227 KB πŸ‘ 1 views

The Cu(I1) binding site of human serum albumin is located on the N-terminal sequence Asp-Ala-His.l-4 It has been shown that the synthetic tripeptide Asp-Ala-His N-methylamide exhibits an affinity towards Cu(I1) ions even higher than that of serum albumin itself.5 In general, i t has been observed th

Functional characterization of an anti-e
✍ StΓ©phane Coulon; Jean-Luc Pellequer; Thierry BlachΓ¨re; Martine Chartier; Elisabe πŸ“‚ Article πŸ“… 2002 πŸ› John Wiley and Sons 🌐 English βš– 288 KB

The high-affinity monoclonal anti-estradiol antibody 9D3 presents a specificity defect towards estradiol-3sulphate and 3-glucuronide conjugates incompatible with use in direct immunoassays. The corresponding single-chain variable fragment (scFv), cloned and produced in E. coli, exhibited a 10-fold l