NMR Studies of Structural Motifs: Protein Folding and Ligand Binding,Used

NMR Studies of Structural Motifs: Protein Folding and Ligand Binding,Used

In Stock
SKU: DADAX3838335775
Brand: LAP Lambert Academic Publishing
Condition: New
$122.78
Quantity
Add to wishlist
Add to compare
Sold by Ergodebooks, an authorized reseller.

Processing time: 1-3 days

US Orders Ships in: 3-5 days

International Orders Ships in: 8-12 days

Return Policy: 15-days return on defective items

Payment Option
Payment Methods

Help

If you have any questions, you are always welcome to contact us. We'll get back to you as soon as possible, withing 24 hours on weekdays.

Customer service

All questions about your order, return and delivery must be sent to our customer service team by e-mail at yourstore@yourdomain.com

Sale & Press

If you are interested in selling our products, need more information about our brand or wish to make a collaboration, please contact us at press@yourdomain.com

NMR of Structural Motifs: The agrin G3 domain is critical in development and maintenance of the neuromuscular junction. G3 binds ?dystroglycan and initiates acetylcholine receptor clustering on myotube membranes. Using NMR spectroscopy, we show both active B8 and inactive B0 isoforms binding sialic acid, heparin, and heparan sulfate and map the binding sites. Ligand dissociation constants were determined by isothermal titration calorimetry. Pulse field gradient diffusion NMR was used to determine heparin binding stoichiometry, 2 protein per heparin. Residual dipolar couplings (RDCs) were used to probe residual denatured OBfold protein structure; folded staphylococcal nuclease (SN) has greater RDC differences. Invariance of denatured SN RDCs had been attributed to robustness of longrange denatured state structure. We show, however, that increased RDC differences in the folded states are a consequence of close packing of native state polypeptide, more consistent with disruption of cooperative structure in folded states than with retention of denatured longrange fold topology. RDCs were used to locate residual secondary structure in denatured OBfold LysN and CspA ?sheets.

⚠️ WARNING (California Proposition 65):

This product may contain chemicals known to the State of California to cause cancer, birth defects, or other reproductive harm.

For more information, please visit www.P65Warnings.ca.gov.

Recently Viewed