scholarly journals Antigenicity and functional properties of β-lactoglobulin conjugated with fructo-oligosaccharides in relation to conformational changes

2013 ◽  
Vol 96 (5) ◽  
pp. 2808-2815 ◽  
Author(s):  
J.Z. Zhong ◽  
Y.J. Xu ◽  
W. Liu ◽  
C.M. Liu ◽  
S.J. Luo ◽  
...  
Keyword(s):  
Functional Properties ◽  
Conformational Changes ◽  
Β Lactoglobulin

scholarly journals Recognition of Conformational Changes in β-Lactoglobulin by Molecularly Imprinted Thin Films

2007 ◽  
Vol 8 (9) ◽  
pp. 2781-2787 ◽  
Author(s):  
Nicholas W. Turner ◽  
Xiao Liu ◽  
Sergey A. Piletsky ◽  
Vladimir Hlady ◽  
David W. Britt
Keyword(s):  
Thin Films ◽  
Conformational Changes ◽  
Molecularly Imprinted ◽  
Β Lactoglobulin

scholarly journals ISOLATION AND STRUCTURE ANALYSIS OF THE MUTANT FORM OF N-TERMINAL CATALYTIC MODULE OF BOS TAURUS TYROSYL-tRNA SYNTHETASE WITH REPLACEMENT OF Trp 40 AND Trp 87 BY ALANINE

2021 ◽  
pp. 27-39
Author(s):  
V. N. Zayets ◽  
L. A. Kolomiiets ◽  
О. Yu. Tsuvarev ◽  
A. I. Kornelyuk
Keyword(s):  
Fluorescence Spectroscopy ◽  
Functional Properties ◽  
Conformational Changes ◽  
Bos Taurus ◽  
Trna Synthetase ◽  
Coli Strain ◽  
Mutant Form ◽  
Compact Structure ◽  
Structural Dynamic ◽  
Cloned Cdna

Aim. Isolation and analysis of the structure of the mutant monotryptophan protein mini BtTyrRS for study of conformational changes of the enzyme at the stage of interaction with tRNA using fluorescence spectroscopy and determination of the effect of tryptophan residues in position 40 and 87 in its structure on the functional properties of the enzyme. Methods. Electrophoresis, metal-chelating affinity chromatography, fluorescence spectroscopy, spatial structure modeling. Results. It was found that the replacement of two codons of Trp by codons of Ala in the cloned cDNA mini BtTyrRS does not affect the synthesis of the mutant form of the enzyme in E. coli strain BL21 (DE3) pLysE. The yield of affinity purified protein on Ni-NTA agarose is on average 3.5 mg per 100 ml of culture medium. Computer modeling of the structure and fluorescence spectroscopy of the monotryptophan form of mini BtTyrRS indicates a compact structure of the mutant enzyme, in which Trp 283 is in an immobilized microenvironment. Conclusions. Affinity purified on Ni-NTA agarose mutant monotryptophan protein mini TyrRS have been obtained which is suitable for fluorescent studies of structural-dynamic and functional properties of the enzyme.

Improvement of Functional Properties of β-Lactoglobulin by Glucose-6-Phosphate Conjugation

2005 ◽  
pp. 409 ◽  
Author(s):  
Takayoshi Aoki ◽  
Tomoko Matsumoto ◽  
Yoshitaka Kako ◽  
Yasuko Kato ◽  
Tsukasa Matsuda
Keyword(s):  
Functional Properties ◽  
Β Lactoglobulin

Human nongastric H+-K+-ATPase: transport properties of ATP1al1 assembled with different β-subunits

2002 ◽  
Vol 283 (1) ◽  
pp. C305-C314 ◽  
Author(s):  
Gilles Crambert ◽  
Jean-Daniel Horisberger ◽  
Nikolai N. Modyanov ◽  
Käthi Geering
Keyword(s):  
Cell Surface ◽  
Transport Properties ◽  
Functional Properties ◽  
Conformational Changes ◽  
Xenopus Oocytes ◽  
Structural Integrity ◽  
Catalytic Subunit ◽  
Α Subunit ◽  
Distinct Effect ◽  
New Evidence

To investigate whether nongastric H+-K+-ATPases transport Na+ in exchange for K+ and whether different β-isoforms influence their transport properties, we compared the functional properties of the catalytic subunit of human nongastric H+-K+-ATPase, ATP1al1 (AL1), and of the Na+-K+-ATPase α1-subunit (α1) expressed in Xenopus oocytes, with different β-subunits. Our results show that βHK and β1-NK can produce functional AL1/β complexes at the oocyte cell surface that, in contrast to α1/β1 NK and α1/βHK complexes, exhibit a similar apparent K+ affinity. Similar to Na+-K+-ATPase, AL1/β complexes are able to decrease intracellular Na+ concentrations in Na+-loaded oocytes, and their K+ transport depends on intra- and extracellular Na+ concentrations. Finally, controlled trypsinolysis reveals that β-isoforms influence the protease sensitivity of AL1 and α1 and that AL1/β complexes, similar to the Na+-K+-ATPase, can undergo distinct K+-Na+- and ouabain-dependent conformational changes. These results provide new evidence that the human nongastric H+-K+-ATPase interacts with and transports Na+ in exchange for K+ and that β-isoforms have a distinct effect on the overall structural integrity of AL1 but influence its transport properties less than those of the Na+-K+-ATPase α-subunit.

scholarly journals Conformational changes induced by polyanions in haemoglobin from Camelus dromedarius. Circular-dichroism study on the oxy derivative

1985 ◽  
Vol 231 (3) ◽  
pp. 793-796 ◽  
Author(s):  
R Santucci ◽  
F Ascoli ◽  
G Amiconi ◽  
A Bertollini ◽  
M Brunori
Keyword(s):  
Functional Properties ◽  
Conformational Changes ◽  
Direct Evidence ◽  
Tertiary Structure ◽  
Camelus Dromedarius ◽  
Local Change ◽  
Inositol Hexakisphosphate ◽  
Human Haemoglobin ◽  
Circular Dichroïsm ◽  
O2 Binding

The c.d. spectrum of oxyhaemoglobin from Camelus dromedarius is significantly affected by the presence of inositol hexakisphosphate. Correlation with O2-binding measurements shows that these dichroic changes parallel the functional properties of the protein. The optical modifications suggest that, in contrast with human haemoglobin, the conformational changes induced by inositol hexakisphosphate on dromedary oxyhaemoglobin are mainly attributable to a local change of the tertiary structure reminiscent of that of the deoxy derivative, the quaternary conformation seeming to be almost unaffected. The results provide direct evidence of the existence on the protein of two distinct sites for polyanions.

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