scholarly journals Effect of Fermentation with Two Molds on Characteristics of Chicken Meat

2021 ◽  
Vol 2021 ◽  
pp. 1-9
Author(s):  
Liping Guo ◽  
Yan Li ◽  
Shengchao Ding ◽  
Baowei Wang ◽  
Yinglian Zhu ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Penicillium Chrysogenum ◽  
Bound Water ◽  
Chicken Meat ◽  
Relative Content ◽  
Granule Formation ◽  
Tyrosine Residues ◽  
Penicillium Nalgiovense

In the present study, we investigated the characteristics of chicken meat fermented with Penicillium nalgiovense and Penicillium chrysogenum. Hardness and springiness gradually decreased, while gumminess gradually increased during fermentation. Fermentation with P. chrysogenum led to higher hardness and lower gumminess than fermentation with P. nalgiovense. Fermentation with two molds resulted in similar microstructure, such as granule formation and fractured myofibril. The highest percentage of secondary structure was ɑ-helix, and tyrosine residues were buried after fermentation. P. nalgiovense-fermented samples contained more bound water, lower relative content of alkanes, and higher relative content of aldehydes than P. chrysogenum-fermented samples.

scholarly journals 124 Bound water and secondary structure of proteins: a new insight in atopic dermatitis?

2016 ◽  
Vol 136 (9) ◽  
pp. S181
Author(s):  
L. Verzeaux ◽  
D. Boudier ◽  
R. Vyumvuhore ◽  
M. Le Guillou ◽  
S. Bordes ◽  
...  
Keyword(s):  
Atopic Dermatitis ◽  
Secondary Structure ◽  
Bound Water ◽  
Secondary Structure Of Proteins ◽  
Structure Of Proteins

Steric accessibility of tyrosine residues in human serum albumin

1979 ◽  
Vol 44 (5) ◽  
pp. 1657-1670 ◽  
Author(s):  
Ladislav Morávek ◽  
Mohamed Ali Saber ◽  
Bedřich Meloun
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Amino Acid Analysis ◽  
Cyanogen Bromide ◽  
Tyrosine Residues ◽  
Steric Accessibility ◽  
The Individual

Human serum albumin was nitrated by an excess of tetranitromethane at pH 8.0. As shown by amino acid analysis, of the 18 tyrosine residues present in albumin about 7-7.5 residues remain unaltered, 9 residues are converted into 3-nitrotyrosine, and 1.2 residue into 3,5-dinitrotyrosine. The nitrated albumin was digested with cyanogen bromide to three fragments which comprise the whole original molecule. The individual fragments were converted into their S-sulfo derivatives and the latter digested with chymotrypsin or stepwise with trypsin and thermolysin. The yellow, nitrotyrosine-containing peptides were isolated from the digest and the positions of nitrated tyrosine residues in albumin thus located. Residues No 30, 148, 150, 161, 334, 341, 401, and 411 were identified as strongly nitrated and residues No 84, 138, 452, and 497 as medium nitrated. Residues No 140, 263, 319, 332, 353, and 367 either react weakly or were not found in nitrated form. Residue No 411 and partly also 161 were converted into 3,5-dinitrotyrosine. The accessibility of the individual tyrosine residues to the nitrating agent is discussed with respect to their positions in disulfide loops and hypothetic parts of the secondary structure of albumin.

Influence of secondary structure on the hydration of serine, threonine and tyrosine residues in proteins

1990 ◽  
Vol 3 (6) ◽  
pp. 495-508 ◽  
Author(s):  
Narmada Thanki ◽  
Janet M. Thornton ◽  
Julia M. Goodfellow
Keyword(s):  
Secondary Structure ◽  
Tyrosine Residues

scholarly journals The insulin receptor juxtamembrane region contains two independent tyrosine/beta-turn internalization signals.

1992 ◽  
Vol 118 (4) ◽  
pp. 831-839 ◽  
Author(s):  
J M Backer ◽  
S E Shoelson ◽  
M A Weiss ◽  
Q X Hua ◽  
R B Cheatham ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Insulin Receptor ◽  
Insulin Binding ◽  
Beta Turns ◽  
Cho Cell ◽  
Beta Turn ◽  
Tyrosine Residues ◽  
Juxtamembrane Region ◽  
Mutant Receptors

We have investigated the role of tyrosine residues in the insulin receptor cytoplasmic juxtamembrane region (Tyr953 and Tyr960) during endocytosis. Analysis of the secondary structure of the juxtamembrane region by the Chou-Fasman algorithms predicts that both the sequences GPLY953 and NPEY960 form tyrosine-containing beta-turns. Similarly, analysis of model peptides by 1-D and 2-D NMR show that these sequences form beta-turns in solution, whereas replacement of the tyrosine residues with alanine destabilizes the beta-turn. CHO cell lines were prepared expressing mutant receptors in which each tyrosine was mutated to phenylalanine or alanine, and an additional mutant contained alanine at both positions. These mutations had no effect on insulin binding or receptor autophosphorylation. Replacements with phenylalanine had no effect on the rate of [125I]insulin endocytosis, whereas single substitutions with alanine reduced [125I]insulin endocytosis by 40-50%. Replacement of both tyrosines with alanine reduced internalization by 70%. These data suggest that the insulin receptor contains two tyrosine/beta-turns which contribute independently and additively to insulin-stimulated endocytosis.

Evolution of Various States of Water in Blended Cementitious Materials

2012 ◽  
Vol 193-194 ◽  
pp. 389-392
Author(s):  
An Ming She ◽  
Wu Yao ◽  
Wan Cheng Yuan
Keyword(s):  
Fly Ash ◽  
Cement Paste ◽  
Bound Water ◽  
Transverse Relaxation Time ◽  
Quantitative Relationship ◽  
Cementitious Materials ◽  
Relative Content ◽  
Cement Matrix ◽  
Transverse Relaxation ◽  
In Series

Low field NMR, as a nondestructure and noninvasive method was employed to study the evolution of various states of water in blended cementious materials added with fly ash during hydration from 1 day to 100 days. The relative content of water held in series of pores in cement matrix, e.g. capillary pore, mesopore and gel pore, was determined based on the quantitative relationship between transverse relaxation time, T2, and pore dimension. The results indicated that the relative content of chemically bound water was higher at long-term cure of 100 days compared with the neat cement paste. The water distributed in various pores was also influenced by the pozzolanic reactions between fly ash and calcium hydroxide. The gel water and mesopore water increased dramatically during the short-term age of 1 to 7 days in blended matrix, but then decreased gradually after 28 days, unlike that in pure cement paste. Due to the lower hydration degree in blended matrix, there was still amount of capillary water residual in paste to supply for the further hydration of fly ash.

Fourier Transform Infrared Spectroscopy Studies of the Secondary Structure in mt-PA6 and mt-PA6 Treated with L-Arginine, L-Asparagine, and (+)-Citrulline in Aqueous Solution

1994 ◽  
Vol 48 (9) ◽  
pp. 1150-1155
Author(s):  
J. L. Kirsch ◽  
R. E. Zimmerman ◽  
L. G. Tensmeyer
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Spectral Data ◽  
Bound Water ◽  
Buffer Solution ◽  
Absorption Region ◽  
Ir Studies ◽  
Vibrational Bands ◽  
Ft Ir ◽  
Spectroscopy Studies

FT-IR studies of the secondary structure of mt-PA6 and mt-PA6 treated with L-arginine, (+)-citrulline, and L-asparagine were carried out in aqueous buffer solution. Spectral subtraction was used to remove the interfering water bands in the amide absorption region, and the amide I absorptions were monitored to investigate changes in the secondary structure of the mt-PA6 induced by the binding of these amino acids. The spectral data showed a narrowing of the amide I absorption of mt-PA6 on treatment with L-arginine, (+)-cirrulline, and L-asparagine. Deconvolution of the amide I absorption revealed vibrational bands characteristic of β-sheet (1632 cm−1), disordered or bound water (1644 cm−1), and turns (1660 cm−1) secondary structures for the mt-PA6. Curve-fitting methods were also used to examine the changes in spectra and secondary structure of the mt-PA6 resulting from amino acid treatment. Analysis of the spectral data shows that loss in intensity of the bands near 1644 and 1660 cm−1 is responsible for the amino acid-induced narrowing of the mt-PA6 amide I absorption. In addition, the spectral data could suggest different binding interactions for L-arginine to mt-PA6 compared to the L-asparagine and (+)-citrulline.

scholarly journals The Effect of Luteolin and Luteoloside on the Secondary Structure of Lysozyme

2021 ◽  
Vol 2021 ◽  
pp. 1-9
Author(s):  
Yu Wu ◽  
Lijian Cui ◽  
Lingling Qu ◽  
Rong Wang ◽  
Ning Chen ◽  
...  
Keyword(s):  
Spectral Analysis ◽  
Biological Activity ◽  
Secondary Structure ◽  
Raman Spectra ◽  
Active Site ◽  
Lysozyme Activity ◽  
Relative Content ◽  
Significant Difference ◽  
Α Helix

The changes of lysozyme conformation in the absence and presence of luteolin and luteoloside were investigated by spectral analysis including fluorescence, UV, CD, Raman, and ATR-FTIR, and the biological activity of lysozyme was investigated by lysozyme assay kit. The results showed that the microenvironment hydrophobicity of lysozyme increased and peptide extension decreased with the addition of luteolin or luteoloside. The α-helix of lysozyme might be influenced by luteolin or luteoloside, and its relative content had a significant difference after adding luteolin or luteoloside by the ATR-FTIR method, which was reconfirmed by CD and Raman spectra. The lysozyme activity changed obviously after adding luteolin or luteoloside. All of the conclusions above indicated the active site of lysozyme in the α-helix might be influenced by luteolin and luteoloside.

Characterization of Tamm-Horsfall Urinary Glycoprotein

1973 ◽  
Vol 31 ◽  
pp. 420-421
Author(s):  
John P. Robinson ◽  
J. David Puett
Keyword(s):  
Electron Microscopy ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Quaternary Structure ◽  
Normal Adult ◽  
Morphological Properties ◽  
Adult Males ◽  
Circular Dichroïsm ◽  
Urinary Glycoprotein

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.

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