Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozyme

Biochemistry ◽  
1992 ◽  
Vol 31 (40) ◽  
pp. 9694-9702 ◽  
Author(s):  
Alain F. Chaffotte ◽  
Yvonne Guillou ◽  
Michel E. Goldberg
Keyword(s):  
Circular Dichroism ◽  
Kinetic Resolution ◽  
Peptide Bond ◽  
Egg White ◽  
Side Chain ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Circular Dichroïsm ◽  
Hen Egg

Circular Dichroism of Hen Egg-white Lysozyme Modified with N-Acetylimidazole*

1972 ◽  
Vol 72 (5) ◽  
pp. 1155-1162 ◽  
Author(s):  
Yoshiko NAKAE ◽  
Kiyoshi IKEDA ◽  
Takachika AZUMA ◽  
Kozo HAMAGUCHI
Keyword(s):  
Circular Dichroism ◽  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Circular Dichroïsm ◽  
Hen Egg

scholarly journals Direct observation of the ZrIV interaction with the carboxamide bond in a noncovalent complex between Hen Egg White Lysozyme and a Zr-substituted Keggin polyoxometalate

2018 ◽  
Vol 74 (11) ◽  
pp. 1348-1354 ◽  
Author(s):  
Laurens Vandebroek ◽  
Luc Van Meervelt ◽  
Tatjana N. Parac-Vogt
Keyword(s):  
Density Functional ◽  
Noncovalent Complex ◽  
Peptide Bond ◽  
Egg White ◽  
Side Chain ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Keggin Polyoxometalate ◽  
Hen Egg

The successful cocrystallization of the noncovalent complex formed between (Et2NH2)8[{α-PW11O39Zr-(μ-OH)(H2O)}2]·7H2O Keggin polyoxometalate (2) and Hen Egg White Lysozyme (HEWL) protein is reported. The resulting structural model revealed interaction between monomeric [Zr(PW11O39)]4−(1), which is a postulated catalytically active species, and the protein in two positions in the asymmetric unit. The first position (occupancy 36%) confirms the previously observed binding sites on the protein surface, whereas the second position (occupancy 14%) provides novel insights into the hydrolytic mechanisms of ZrIV-substituted polyoxometalates. The new interaction site occurs at the Asn65 residue, which is directly next to the Asp66–Gly67 peptide bond that was identified recently as a cleavage site in the polyoxometalate-catalysed hydrolysis of HEWL. Furthermore, in this newly discovered binding site, the monomeric polyoxometalate 1 is observed to bind directly to the side chain of the Asn65 residue. This binding of ZrIV as a Lewis-acid metal to the carbonyl O atom of the Asn65 side chain is very similar to the intermediate state proposed in density functional theory (DFT) studies in which ZrIV activates the peptide bond via interaction with its carbonyl O atom, and can be thus regarded as a model for interaction between ZrIV and a peptide bond.

Methylation at lysine side chain of hen egg white lysozyme (HEWL) promote its amyloid formation

2011 ◽  
Vol 44 (13) ◽  
pp. S23-S24
Author(s):  
Ostadi Hassan ◽  
Shariat Sajjad ◽  
Ali Akbar Meratan ◽  
Ali Es-haghi ◽  
Mohsen Nemat-Gorgani
Keyword(s):  
Egg White ◽  
Side Chain ◽  
Amyloid Formation ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Lysine Side Chain ◽  
Hen Egg White ◽  
Hen Egg

Inactivation of hen egg-white lysozyme. The azide radical

1997 ◽  
Vol 94 ◽  
pp. 356-364 ◽  
Author(s):  
M Faraggi ◽  
E Bettelheim ◽  
M Weinstein
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg
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