TL;DR: In this article, a single polypeptide chain binding molecule has been proposed which has binding specificity and affinity substantially similar to the binding specificity of the light and heavy chain aggregate variable region of an antibody.
Abstract: The invention pertains to a single polypeptide chain binding molecule which has binding specificity and affinity substantially similar to the binding specificity and affinity of the light and heavy chain aggregate variable region of an antibody, to genetic sequences coding therefor, and to recombinant DNA methods of producing such molecule and uses for such molecule.
TL;DR: Crystallographic resolution of bound carbon dioxide in a porous solid validates methods of theoretically predicting binding behavior and bodes well for the theory-aided development of amine-based CO2 sorbents.
Abstract: Understanding the molecular details of CO(2)-sorbent interactions is critical for the design of better carbon-capture systems. Here we report crystallographic resolution of CO(2) molecules and their binding domains in a metal-organic framework functionalized with amine groups. Accompanying computational studies that modeled the gas sorption isotherms, high heat of adsorption, and CO(2) lattice positions showed high agreement on all three fronts. The modeling apportioned specific binding interactions for each CO(2) molecule, including substantial cooperative binding effects among the guest molecules. The validation of the capacity of such simulations to accurately model molecular-scale binding bodes well for the theory-aided development of amine-based CO(2) sorbents. The analysis shows that the combination of appropriate pore size, strongly interacting amine functional groups, and the cooperative binding of CO(2) guest molecules is responsible for the low-pressure binding and large uptake of CO(2) in this sorbent material.
TL;DR: Atomic resolution structures of nicotine and carbamylcholine binding to AChBP, a water-soluble homolog of the ligand binding domain of nicotinic receptors and their family members, GABAA,GABAC, 5HT3 serotonin, and glycine receptors are presented.
TL;DR: The various elements in this model for the binding of steroidal estrogens by the estrogen receptor are consistent with evidence emerging from the crystal structures of related nuclear hormone receptor ligand complexes.
TL;DR: It is shown that allostery can be mediated exclusively by transmitted changes in protein motions, and this work characterized the negatively cooperative binding of cAMP to the dimeric catabolite activator protein (CAP) at discrete conformational states.
Abstract: Allosteric interactions are typically considered to proceed through a series of discrete changes in bonding interactions that alter the protein conformation. Here we show that allostery can be mediated exclusively by transmitted changes in protein motions. We have characterized the negatively cooperative binding of cAMP to the dimeric catabolite activator protein (CAP) at discrete conformational states. Binding of the first cAMP to one subunit of a CAP dimer has no effect on the conformation of the other subunit. The dynamics of the system, however, are modulated in a distinct way by the sequential ligand binding process, with the first cAMP partially enhancing and the second cAMP completely quenching protein motions. As a result, the second cAMP binding incurs a pronounced conformational entropic penalty that is entirely responsible for the observed cooperativity. The results provide strong support for the existence of purely dynamics-driven allostery.