Model compounds for metal–protein interaction: crystal structures of four silver(II) complexes with glycine, glycylglycine, and imidazole

1971 ◽  
Vol 0 (17) ◽  
pp. 1016-1017 ◽  
Author(s):  
C. B. Acland ◽  
H. C. Freeman
Keyword(s):  
Crystal Structures ◽  
Protein Interaction ◽  
Model Compounds

Model Compounds for Metal–protein Interaction: Crystal Structures of two Glycylglycylglycine–copper Complexes

Nature ◽  
1962 ◽  
Vol 194 (4835) ◽  
pp. 1237-1239 ◽  
Author(s):  
T. COOPER ◽  
H. C. FREEMAN ◽  
G. ROBINSON ◽  
J. C. SCHOONE
Keyword(s):  
Crystal Structures ◽  
Protein Interaction ◽  
Copper Complexes ◽  
Model Compounds

Crystal structures and phase transition behavior of Poly(nonamethylene terephthalamide) and its model compounds

Polymer ◽  
2017 ◽  
Vol 116 ◽  
pp. 378-394 ◽  
Author(s):  
Hiroko Yamamoto ◽  
Kohji Tashiro ◽  
Kiyotaka Ishino ◽  
Masahide Takahashi ◽  
Ryokei Endo ◽  
...  
Keyword(s):  
Phase Transition ◽  
Crystal Structures ◽  
Phase Transition Behavior ◽  
Model Compounds ◽  
Transition Behavior

Single-Crystal Structures of Model Compounds for Poly(2,5-dialkoxy-1,4-phenylenevinylene)

1999 ◽  
Vol 11 (8) ◽  
pp. 2103-2106 ◽  
Author(s):  
Ulf Stalmach ◽  
Dieter Schollmeyer ◽  
Herbert Meier
Keyword(s):  
Single Crystal ◽  
Crystal Structures ◽  
Model Compounds ◽  
Single Crystal Structures

scholarly journals Uncovering the basis of protein-protein interaction specificity with a combinatorially complete library

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Thuy-Lan V Lite ◽  
Robert A Grant ◽  
Isabel Nocedal ◽  
Megan L Littlehale ◽  
Monica S Guo ◽  
...  
Keyword(s):  
Molecular Recognition ◽  
Crystal Structures ◽  
Protein Interaction ◽  
Bacterial Toxin ◽  
General Nature ◽  
Primary Sequence ◽  
Wild Type ◽  
Mutational Robustness ◽  
Protein Protein Interaction ◽  
Interface Residues

Protein-protein interaction specificity is often encoded at the primary sequence level. However, the contributions of individual residues to specificity are usually poorly understood and often obscured by mutational robustness, sequence degeneracy, and epistasis. Using bacterial toxin-antitoxin systems as a model, we screened a combinatorially complete library of antitoxin variants at three key positions against two toxins. This library enabled us to measure the effect of individual substitutions on specificity in hundreds of genetic backgrounds. These distributions allow inferences about the general nature of interface residues in promoting specificity. We find that positive and negative contributions to specificity are neither inherently coupled nor mutually exclusive. Further, a wild-type antitoxin appears optimized for specificity as no substitutions improve discrimination between cognate and non-cognate partners. By comparing crystal structures of paralogous complexes, we provide a rationale for our observations. Collectively, this work provides a generalizable approach to understanding the logic of molecular recognition.

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