Investigation of DMSO-Induced Conformational Transitions in Human Serum Albumin Using Two-Dimensional Raman Optical Activity Spectroscopy

Chirality ◽  
2014 ◽  
Vol 26 (9) ◽  
pp. 497-501 ◽  
Author(s):  
Andrea N. L. Batista ◽  
João M. Batista ◽  
Lorna Ashton ◽  
Vanderlan S. Bolzani ◽  
Maysa Furlan ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Optical Activity ◽  
Conformational Transitions ◽  
Two Dimensional ◽  
Raman Optical Activity

Loop structure in human serum albumin from Raman optical activity

1998 ◽  
Vol 29 (1) ◽  
pp. 67-71 ◽  
Author(s):  
Junji Teraoka ◽  
Alasdair F. Bell ◽  
Lutz Hecht ◽  
Laurence D. Barron
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Optical Activity ◽  
Loop Structure ◽  
Raman Optical Activity

Two-dimensional gel electrophoresis and immunoblotting of human serum albumin modified by reaction with penicillins

1995 ◽  
Vol 16 (1) ◽  
pp. 851-853 ◽  
Author(s):  
Barbara Marzocchi ◽  
Barbara Magi ◽  
Luca Bini ◽  
Carla Cellesi ◽  
Aldo Rossolini ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

Inhibition of Human Serum Albumin Fibrillation by Two-Dimensional Nanoparticles

2017 ◽  
Vol 121 (22) ◽  
pp. 5474-5482 ◽  
Author(s):  
Sudipta Bag ◽  
Rishav Mitra ◽  
Sunando DasGupta ◽  
Swagata Dasgupta
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Two Dimensional

scholarly journals The fatty-acid-induced conformational states of human serum albumin investigated by means of multiple co-binding of protons and oleic acid

1988 ◽  
Vol 250 (2) ◽  
pp. 443-446 ◽  
Author(s):  
J H M Dröge ◽  
L H M Janssen ◽  
J Wilting
Keyword(s):  
Oleic Acid ◽  
Fatty Acid ◽  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Conformational Transitions ◽  
Amino Acid Residues ◽  
Ph Stat

The binding of oleic acid to human serum albumin causes progressive changes in (a) the pK of some amino acid residues, as detected by pH-stat titration and (b) the induced molar ellipticities of albumin-bound drugs (diazepam and oxyphenbutazone), as measured by c.d. It is concluded that albumin undergoes several conformational transitions as the amount of oleic acid bound increases from 0 to about 9 molecules/molecule of protein. At least three different conformations of the protein seem to be involved. These conformations can be linked with the three classes of oleic acid-binding sites on albumin.

Ultrafast Solvation Dynamics of Human Serum Albumin:  Correlations with Conformational Transitions and Site-Selected Recognition

2006 ◽  
Vol 110 (21) ◽  
pp. 10540-10549 ◽  
Author(s):  
Weihong Qiu ◽  
Luyuan Zhang ◽  
Oghaghare Okobiah ◽  
Yi Yang ◽  
Lijuan Wang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Transitions ◽  
Solvation Dynamics
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