The kinetics of the quantitative, symmetry allowed, reverse electron demand cycloadditions of the pseudo-1,3-dipole SNS+with alkynes and nitriles; the preparation and X-ray crystal structures of NCCSNSCHAsF6and SNSNC–CNSNS(AsF6)2: the precursor to a new class of S2N2C–CN2S2n+(n= 0,1,2) bicyclics

1991 ◽  
pp. 369-371 ◽  
Author(s):  
Simon Parsons ◽  
Jack Passmore ◽  
Melbourne J. Schriver ◽  
Peter S. White
Keyword(s):  
Crystal Structures ◽  
X Ray ◽  
New Class ◽  
Kinetics Of ◽  
Electron Demand

The Through-Bond Interaction of a Sulfur Lone Pair with Oxygenated Substituents in the Thiacyclohexane Framework

2005 ◽  
Vol 58 (7) ◽  
pp. 531
Author(s):  
Laura Andrau ◽  
Jonathan M. White
Keyword(s):  
Low Temperature ◽  
Crystal Structures ◽  
Bond Distance ◽  
Lone Pair ◽  
X Ray ◽  
Ester Derivative ◽  
Bond Interaction ◽  
Derivatives Of ◽  
Electron Demand

Low-temperature X-ray crystal structures were determined on a range of derivatives of 4-thiacyclohexanol 5a of varying electron demand with a view to finding evidence for a through-bond interaction between the sulfur lone pair and the oxygenated substituent. In contrast to earlier suggestions, plots of C–OR bond distance versus pKa (ROH) showed that any interaction between the sulfur and the OR group is unlikely to be of a through-bond origin. Furthermore, unimolecular solvolysis rate measurements on the nosylate ester derivative 5g showed that the sulfur actually retards the reaction slightly in comparison with the corresponding sulfur-free analogue 6.

scholarly journals The Domain Structure of ICAM-1 and the Kinetics of Binding to Rhinovirus

1998 ◽  
Vol 72 (7) ◽  
pp. 6244-6246 ◽  
Author(s):  
José M. Casasnovas ◽  
Joanna K. Bickford ◽  
Timothy A. Springer
Keyword(s):  
Crystal Structures ◽  
Domain Structure ◽  
Adhesion Molecule ◽  
Extracellular Domain ◽  
Intercellular Adhesion ◽  
Intercellular Adhesion Molecule ◽  
Intercellular Adhesion Molecule 1 ◽  
X Ray ◽  
Kinetics Of

ABSTRACT Fragments of intercellular adhesion molecule 1 (ICAM- 1) containing only the two most N terminal of its five immunoglobulin SF domains bind to rhinovirus 3 with the same affinity and kinetics as a fragment with the entire extracellular domain. The fully active two-domain fragments contain 5 or 14 more residues than a previously described fragment that is only partially active. Comparison of X-ray crystal structures show differences at the bottom of domain 2. Four different glycoforms of ICAM- 1 bind with identical kinetics.

Sign in / Sign up

Export Citation Format

Share Document