Adsorption of fibrinogen on a biomedical-grade stainless steel 316LVM surface: a PM-IRRAS study of the adsorption thermodynamics, kinetics and secondary structure changes

2008 ◽  
Vol 10 (18) ◽  
pp. 2502 ◽  
Author(s):  
Marie-Josee Desroches ◽  
Sasha Omanovic
Keyword(s):  
Stainless Steel ◽  
Secondary Structure ◽  
Adsorption Thermodynamics ◽  
Structure Changes

scholarly journals Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 359 ◽  
Author(s):  
Usoltsev ◽  
Sitnikova ◽  
Kajava ◽  
Uspenskaya
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Ftir Spectroscopy ◽  
Conformational Changes ◽  
Data Interpretation ◽  
Random Coil ◽  
Helical Conformation ◽  
Structure Changes

Human serum albumin (HSA) is the most abundant protein in blood plasma. HSA is involved in the transport of hormones, fatty acids, and some other compounds, maintenance of blood pH, osmotic pressure, and many other functions. Although this protein is well studied, data about its conformational changes upon different denaturation factors are fragmentary and sometimes contradictory. This is especially true for FTIR spectroscopy data interpretation. Here, the effect of various denaturing agents on the structural state of HSA by using FTIR spectroscopy in the aqueous solutions was systematically studied. Our data suggest that the second derivative deconvolution method provides the most consistent interpretation of the obtained IR spectra. The secondary structure changes of HSA were studied depending on the concentration of the denaturing agent during acid, alkaline, and thermal denaturation. In general, the denaturation of HSA in different conditions is accompanied by a decrease in α-helical conformation and an increase in random coil conformation and the intermolecular β-strands. Meantime, some variation in the conformational changes depending on the type of the denaturation agent were also observed. The increase of β-structural conformation suggests that HSA may form amyloid-like aggregates upon the denaturation.

scholarly journals Structural and compositional changes of whey protein and blueberry juice fermented using Lactobacillus plantarum or Lactobacillus casei during fermentation

RSC Advances ◽  
2021 ◽  
Vol 11 (42) ◽  
pp. 26291-26302
Author(s):  
Wang Wen-qiong ◽  
Zhang Jie-long ◽  
Yu Qian ◽  
Zhou Ji-yang ◽  
Lu Mao-lin ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Secondary Structure ◽  
Whey Protein ◽  
Lactobacillus Plantarum ◽  
Lactobacillus Casei ◽  
Schematic Diagram ◽  
Blueberry Juice ◽  
Structure Changes ◽  
Compositional Changes

A possible schematic diagram to show how the secondary structure changes which the whey protein and blueberry juice interaction after Lactobacillus casei or Lactobacillus plantarum fermentation was inferred from the structural analysis results.

scholarly journals U2 snRNA structure is influenced by SF3A and SF3B proteins but not by SF3B inhibitors

2021 ◽  
Author(s):  
Veronica K Urabe ◽  
Meredith Stevers ◽  
Arun K Ghosh ◽  
Melissa S. Jurica
Keyword(s):  
Secondary Structure ◽  
Complex Formation ◽  
Small Molecule ◽  
Branch Point ◽  
Reactivity Pattern ◽  
U2 Snrna ◽  
Chemical Probing ◽  
Rna Conformation ◽  
Structure Changes ◽  
U2 Snrnp

U2 snRNP is an essential component of the spliceosome. It is responsible for branch point recognition in the spliceosome A-complex via base-pairing of U2 snRNA with an intron to form the branch helix. Small molecule inhibitors target the SF3B component of the U2 snRNP and interfere with A-complex formation during spliceosome assembly. We previously found that the first SF3B inhibited-complex is less stable than A-complex and hypothesized that SF3B inhibitors interfere with U2 snRNA secondary structure changes required to form the branch helix. Using RNA chemical modifiers, we probed U2 snRNA structure in A-complex and SF3B inhibited splicing complexes. The reactivity pattern for U2 snRNA in the SF3B inhibited-complex is indistinguishable from that of A-complex, suggesting that they have the same secondary structure conformation, including the branch helix. This observation suggests SF3B inhibited-complex instability does not stem from an alternate RNA conformation and instead points to the inhibitors interfering with protein component interactions that normally stabilize U2 snRNP's association with an intron. In addition, we probed U2 snRNA in the free U2 snRNP in the presence of SF3B inhibitor and again saw no differences. However, increased protection of nucleotides upstream of Stem I in the absence of SF3A and SF3B proteins suggests a change of secondary structure at the very 5′ end of U2 snRNA. Chemical probing of synthetic U2 snRNA in the absence of proteins results in similar protections and predicts a previously uncharacterized extension of Stem I. Because this stem must be disrupted for SF3A and SF3B proteins to stably join the snRNP, the structure has the potential to influence snRNP assembly and recycling after spliceosome disassembly.

Secondary Structure Changes of Tubulin Induced by Navelbine as Studied by FT-IR

1993 ◽  
pp. 149-150
Author(s):  
N. Allam ◽  
J. M. Millot ◽  
D. Leynadier ◽  
V. Peyrot ◽  
C. Briand ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Structure Changes ◽  
Ft Ir
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