Ultrafast spectroscopic investigations of the relaxation dynamics of a new class of water-soluble Coumarins

1996 ◽  
Author(s):  
L. Cassara ◽  
T. Gustavsson ◽  
S. Pommeret ◽  
J.-C. Mialocq ◽  
J. Chalom ◽  
...  
Keyword(s):  
Water Soluble ◽  
Relaxation Dynamics ◽  
New Class ◽  
Spectroscopic Investigations

Water-soluble macrocyclic paddlanes and propellane as a new class of host molecules

1984 ◽  
pp. 2681 ◽  
Author(s):  
Yoshito Tobe ◽  
Hisashi Fujita ◽  
Itsuyo Wakaki ◽  
Kaoru Terashima ◽  
Kazuya Kobiro ◽  
...  
Keyword(s):  
Water Soluble ◽  
New Class ◽  
Host Molecules

scholarly journals AplA, a Member of a New Class of Phycobiliproteins Lacking a Traditional Role in Photosynthetic Light Harvesting

2004 ◽  
Vol 186 (21) ◽  
pp. 7420-7428 ◽  
Author(s):  
Beronda L. Montgomery ◽  
Elena Silva Casey ◽  
Arthur R. Grossman ◽  
David M. Kehoe
Keyword(s):  
Amino Acid ◽  
Tertiary Structure ◽  
Light Harvesting ◽  
Water Soluble ◽  
Amino Acid Residues ◽  
Subunit Interactions ◽  
Traditional Role ◽  
Light Harvesting Complexes ◽  
Fremyella Diplosiphon ◽  
New Class

ABSTRACT All known phycobiliproteins have light-harvesting roles during photosynthesis and are found in water-soluble phycobilisomes, the light-harvesting complexes of cyanobacteria, cyanelles, and red algae. Phycobiliproteins are chromophore-bearing proteins that exist as heterodimers of α and β subunits, possess a number of highly conserved amino acid residues important for dimerization and chromophore binding, and are invariably 160 to 180 amino acids long. A new and unusual group of proteins that is most closely related to the allophycocyanin members of the phycobiliprotein superfamily has been identified. Each of these proteins, which have been named allophycocyanin-like (Apl) proteins, apparently contains a 28-amino-acid extension at its amino terminus relative to allophycocyanins. Apl family members possess the residues critical for chromophore interactions, but substitutions are present at positions implicated in maintaining the proper α-β subunit interactions and tertiary structure of phycobiliproteins, suggesting that Apl proteins are able to bind chromophores but fail to adopt typical allophycocyanin conformations. AplA isolated from the cyanobacterium Fremyella diplosiphon contained a covalently attached chromophore and, although present in the cell under a number of conditions, was not detected in phycobilisomes. Thus, Apl proteins are a new class of photoreceptors with a different cellular location and structure than any previously described members of the phycobiliprotein superfamily.

Water-soluble pillar[5]arenes: A new class of plant growth regulators

2019 ◽  
Vol 60 (34) ◽  
pp. 150949 ◽  
Author(s):  
Liqing Shangguan ◽  
Bingbing Shi ◽  
Qi Chen ◽  
Yang Li ◽  
Huangtianzhi Zhu ◽  
...  
Keyword(s):  
Plant Growth ◽  
Plant Growth Regulators ◽  
Growth Regulators ◽  
Water Soluble ◽  
New Class
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