scholarly journals Rat brain Thy-1 glycoprotein. The amino acid sequence, disulphide bonds and an unusual hydrophobic region

1981 ◽  
Vol 195 (1) ◽  
pp. 15-30 ◽  
Author(s):  
D G Campbell ◽  
J Gagnon ◽  
K B Reid ◽  
A F Williams
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Rat Brain ◽  
Amino Terminus ◽  
Membrane Glycoprotein ◽  
Hydrophobic Properties ◽  
Hydrophobic Region ◽  
Disulphide Bonds ◽  
Extended Sequence ◽  
Hydrophobic Amino Acids

The full sequence of the Thy-1 membrane glycoprotein of rat brain is reported. The sequence was determined from tryptic and V-8 proteinase peptides and consisted of 111 amino acids. The amino terminus was blocked and consisted of a pyroglutamic acid residue. The molecule contained two disulphide bonds, namely Cys-9--Cys-111 and Cys-19--Cys-85. Three N-linked amino sugars were located at Asn-23, Asn-74 and Asn-98. In each case the sequence on the C-terminal side of the attachment point was Asn-Xaa-Thr as would be expected for N-linkage. The C-terminal peptides were unusual, in that they were either obtained in a highly aggregated form, or could only be purified after binding to Brij 96 micelles. Thus they appeared to have hydrophobic properties, yet did not contain any extended sequence of hydrophobic amino acids. Other unusual features of the C-terminal peptides were the presence of unidentified ninhydrin-positive material and of glucosamine and galactosamine. The C-terminal residue has not been directly identified but Cys-111 is the last conventional amino acid. It is suggested that the hydrophobic properties of the C-terminal peptides may be due to the linkage of lipid. The sequence of the Thy-1 glycoprotein showed homologies with immunoglobulin domains. This relationship is examined in detail in the paper following [Cohen et al. (1981) Biochem. J. 193, 000--000].

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

Food Intake Regulation: Amino Acid Toxicity and Changes in Rat Brain and Plasma Amino Acids

1973 ◽  
Vol 103 (4) ◽  
pp. 608-617 ◽  
Author(s):  
Y. Peng ◽  
J. Gubin ◽  
A. E. Harper ◽  
M. G. Vavich ◽  
A. R. Kemmerer
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Food Intake ◽  
Rat Brain ◽  
Plasma Amino Acids ◽  
Food Intake Regulation ◽  
Acid Toxicity ◽  
Intake Regulation

scholarly journals Characterization of human torsinA and its dystonia-associated mutant form

2003 ◽  
Vol 374 (1) ◽  
pp. 117-122 ◽  
Author(s):  
Zhonghua LIU ◽  
Anna ZOLKIEWSKA ◽  
Michal ZOLKIEWSKI
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Signal Sequence ◽  
Eukaryotic Cells ◽  
Membrane Association ◽  
S2 Cells ◽  
Wild Type ◽  
Hydrophobic Region ◽  
Terminal Amino ◽  
Membrane Anchoring

Deletion of a single glutamate in torsinA correlates with early-onset dystonia, the most severe form of a neurological disorder characterized by uncontrollable muscle contractions. TorsinA is targeted to the ER (endoplasmic reticulum) in eukaryotic cells. We investigated the processing and membrane association of torsinA and the dystonia-associated Glu-deletion mutant (torsinAΔE). We found that the signal sequence of torsinA (residues 1–20 from the 40 amino-acid long N-terminal hydrophobic region) is cleaved in Drosophila S2 cells, as shown by the N-terminal sequencing after partial protein purification. TorsinA is not secreted from S2 cells. Consistently, sodium carbonate extraction and Triton X-114 treatment showed that torsinA is associated with the ER membrane in CHO (Chinese-hamster ovary) cells. In contrast, a variant of torsinA that contains the native signal sequence without the hydrophobic region Ile24–Pro40 does not associate with the membranes in CHO cells, and a truncated torsinA without the 40 N-terminal amino acids is secreted in the S2 culture. Thus the 20-amino-acid-long hydrophobic segment in torsinA, which remains at the N-terminus after signal-peptide cleavage, is responsible for the membrane anchoring of torsinA. TorsinAΔE showed similar cleavage of the 20 N-terminal amino acids and membrane association properties similar to wild-type torsinA but, unlike the wild-type, torsinAΔE was not secreted in the S2 culture even after deletion of the membrane-anchoring segment. This indicates that the dystonia-associated mutation produces a structurally distinct, possibly misfolded, form of torsinA, which cannot be properly processed in the secretory pathway of eukaryotic cells.

scholarly journals Increased thermal stability of proteins in the presence of amino acids

1994 ◽  
Vol 303 (1) ◽  
pp. 147-153 ◽  
Author(s):  
S Taneja ◽  
F Ahmad
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Cytochrome C ◽  
Thermal Denaturation ◽  
Thermal Transition ◽  
Native Protein ◽  
Guanidinium Chloride ◽  
Isoleucine Leucine ◽  
Hydrophobic Amino Acids ◽  
Thermal Stability Of

This study is a systematic attempt to understand the roles of osmolytes in protecting proteins against denaturing stress. Thermal denaturation of cytochrome c has been studied in the presence of various concentrations of all L-amino acids that are more hydrophobic than glycine and have a solubility of 0.1 M or higher in water at 25 degrees C. The basic observations are as follows. (1) Arginine and histidine destabilize the native protein; both Tm (the midpoint of thermal transition) and delta GDH2O (25 degrees C) (the Gibbs energy of stabilization) decrease with increasing amino acid concentration. (2) Isoleucine, leucine and phenylalanine have no effect on Tm and deltaGDH2O (25 degrees C). (3) Valine and less hydrophobic amino acids stabilize the protein in terms of Tm but deltaGDH2O (25 degrees C) is unchanged. This observation was confirmed by the study of isothermal denaturation of cytochrome c by guanidinium chloride which suggested that delta GDH2O is independent of osmolyte concentration, but Cm (the midpoint of transition) is increased in their presence. (4) In the case of stabilizers, change in Tm/mol of amino acid decreases with increasing hydrophobicity of these osmolytes.

Amino-terminal TACE prodomain attenuates TNFR2 cleavage independently of the cysteine switch

2005 ◽  
Vol 288 (6) ◽  
pp. L1132-L1138 ◽  
Author(s):  
Caitriona A. Buckley ◽  
Farshid N. Rouhani ◽  
Maryann Kaler ◽  
Barbara Adamik ◽  
Feras I. Hawari ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Inhibitory Activity ◽  
Catalytic Domain ◽  
Amino Terminus ◽  
Mucin Production ◽  
Inactive State ◽  
Amino Terminal ◽  
Switch Mechanism ◽  
Cysteine Switch

TNF-α-converting enzyme (TACE, ADAM17) cleaves membrane-associated cytokines and receptors and thereby regulates inflammatory and immune events, as well as lung development and mucin production. For example, the TACE-mediated cleavage of the type II 75-kDa TNF receptor (TNFR2) generates a soluble TNF-binding protein that modulates TNF bioactivity. TACE is synthesized as a latent proenzyme that is retained in an inactive state via an interaction between its prodomain and catalytic domain. Although the formation of an intramolecular bond between a cysteine in the prodomain and a zinc atom in the catalytic site had been thought to mediate this inhibitory activity, it was recently reported that the cysteine-switch motif is not required. Here, we hypothesized that the amino terminus of the TACE prodomain might contribute to the ability of the prodomain to maintain TACE in an inactive state independently of a cysteine-switch mechanism. We synthesized a 37-amino acid peptide corresponding to TACE amino acids 18–54 (N-TACE18–54) and assessed whether it possessed TACE inhibitory activity. In an in vitro model assay system, N-TACE18–54 attenuated TACE-catalyzed cleavage of a TNFR2:Fc substrate. Furthermore, N-TACE18–54 inhibited constitutive TNFR2 shedding from a human monocytic cell line by 42%. A 19-amino acid, leucine-rich domain, corresponding to TACE amino acids 30–48, demonstrated partial inhibitory activity. In summary, we have identified a subdomain within the amino terminus of the TACE prodomain that attenuates TACE catalytic activity independently of a cysteine-switch mechanism, which provides new insight into the regulation of TACE enzymatic activity.

scholarly journals Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases

2009 ◽  
Vol 390 (3) ◽  
Author(s):  
Takayuki K. Nemoto ◽  
Toshio Ono ◽  
Yu Shimoyama ◽  
Shigenobu Kimura ◽  
Yuko Ohara-Nemoto
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protease Activity ◽  
Binding Pocket ◽  
Catalytic Triad ◽  
Amino Acid Residues ◽  
Proteolytic Activities ◽  
Hydrophobic Amino Acids ◽  
The Difference

Abstract Staphylococcus aureus, Staphylococcus epidermidis, and Staphylococcus warneri secrete glutamyl endopeptidases, designated GluV8, GluSE, and GluSW, respectively. The order of their protease activities is GluSE<GluSW<<GluV8. In the present study, we investigated the mechanism that causes these differences. Expression of chimeric proteins between GluV8 and GluSE revealed that the difference is primarily attributed to amino acid residues 170–195, which define the intrinsic protease activity, and additionally to residues 119–169, which affect the proteolytic sensitivity. Among nine substitutions present in residues 170–195 of the three proteases, the substitutions at positions 185, 188, and 189 were responsible for the changes in their activities, and the combination of W185, V188, and P189, which naturally occurs in GluV8, exerts the highest protease activity. W185 and P189 were indispensable for full activity, but V188 could be replaced by hydrophobic amino acids. These three amino acid residues appear to create a substrate-binding pocket together with the catalytic triad and the N-terminal V1, and therefore define the K m values of the proteases. We also describe a method to produce a chimeric form of GluSE and GluV8 that is resistant to proteolysis, and therefore possesses 4-fold higher activity than the wild-type recombinant GluV8.

scholarly journals Extraction and Characterization of “Batuan” [Garcinia binucao (Blco.) Choisy] Seed Protein

2014 ◽  
pp. 89-103 ◽  
Author(s):  
Elizabeth Quevedo ◽  
Marivic Lacsamana ◽  
Antonio Laurena
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Seed Protein ◽  
Seed Proteins ◽  
Essential Amino Acids ◽  
Food Supplement ◽  
Seed Meal ◽  
Molecular Weights ◽  
Hydrophobic Amino Acids ◽  
Amino Acid Score

“Batuan” [Garcinia binucao (Blco.) Choisy], an indigenous, lesser known member of the Gutifferae family with export potential is underutilized and understudied. The present study was carried out to extract and characterize the protein in “batuan” [Garcinia binucao (Blco.) Choisy] seeds for nutritional quality assessment. Protein content of “batuan” seed meal was 8.9 ± 0.59% dry basis. Solubility fractionation of “batuan” seed meal showed globulin and glutelin as the major seed proteins. SDS-PAGE resolved the globulin and glutelin into three groups of polypeptides with molecular weights of about 20 – 54 kDa. Amino acid analysis revealed that seed protein contained all the essential amino acids with leucine as the most abundant while tryptophan, the least. “Batuan” seed proteins were mostly made up of acidic and hydrophobic amino acids with glutamic acid (2.67%) as the highest. Nutritional assessments including E/T (38.4%), amino acid score (1.6%), predicted PER (3.2-3.7) and estimated BV (98.3%) suggested that the seed proteins are of good quality. Hence, “batuan” seeds has a promising potential as an important sources of valuable proteins and amino acids for use as food supplement/enhancing ingredient.

scholarly journals DLPacker: Deep Learning for Prediction of Amino Acid Side Chain Conformations in Proteins

2021 ◽  
Author(s):  
Mikita Misiura ◽  
Raghav Shroff ◽  
Ross Thyer ◽  
Anatoly Kolomeisky
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Design ◽  
Structure Prediction ◽  
Deep Neural Networks ◽  
Side Chain ◽  
Amino Acid Side Chain ◽  
Image Transformation ◽  
Hydrophobic Amino Acids ◽  
Chain Conformations

Prediction of side chain conformations of amino acids in proteins (also termed 'packing') is an important and challenging part of protein structure prediction with many interesting applications in protein design. A variety of methods for packing have been developed but more accurate ones are still needed. Machine learning (ML) methods have recently become a powerful tool for solving various problems in diverse areas of science, including structural biology. In this work we evaluate the potential of Deep Neural Networks (DNNs) for prediction of amino acid side chain conformations. We formulate the problem as image-to-image transformation and train a U-net style DNN to solve the problem. We show that our method outperforms other physics-based methods by a significant margin: reconstruction RMSDs for most amino acids are about 20% smaller compared to SCWRL4 and Rosetta Packer with RMSDs for bulky hydrophobic amino acids Phe, Tyr and Trp being up to 50% smaller.

scholarly journals Development of natural and unnatural amino acid delivery systems against hookworm infection

2020 ◽  
Vol 3 (1) ◽  
pp. 471-482 ◽  
Author(s):  
Stacey Bartlett ◽  
Mariusz Skwarczynski ◽  
Xin Xie ◽  
Istvan Toth ◽  
Alex Loukas ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Single Molecule ◽  
Cell Epitope ◽  
Unnatural Amino Acid ◽  
Nippostrongylus Brasiliensis ◽  
Peptide Fragments ◽  
Specific Pathogen ◽  
Hydrophobic Amino Acids ◽  
Natural Amino Acids

Peptide-based vaccines consist of short antigen fragments derived from a specific pathogen. Alone, these peptide fragments are poorly or non-immunogenic; however, when incorporated into a proper delivery system, they can trigger strong immune responses. To eliminate the need for toxic and often ineffective oral adjuvants, we designed single molecule-based self-adjuvating vaccines against hookworms using natural and unnatural hydrophobic amino acids. Two vaccine conjugates were synthesized, consisting of B-cell epitope p3, derived from the hookworm Na-APR-1 protein; universal T-helper peptide P25; and either double copies of unnatural lipoamino acid (2-amino-D,L-eicosanoic acid), or ten copies of the natural amino acid leucine. After challenge with the model hookworm, Nippostrongylus brasiliensis, mice orally immunized with the conjugates, but without adjuvant, generated antibody responses against the hookworm epitope, resulting in significantly reduced worm and egg burdens compared to control mice. We have demonstrated that vaccine nanoparticles composed exclusively of natural amino acids can be effective even when administered orally.

scholarly journals Improvement of Functional Properties of Jack Bean (Canavalia ensiformis) Flour by Germination and Its Relation to Amino Acids Profile

2021 ◽  
Vol 9 (3) ◽  
pp. 812-822
Author(s):  
Bayu Kanetro ◽  
Muhamad Riyanto ◽  
Dwiyati Pujimulyani ◽  
Nurul Huda
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Functional Properties ◽  
Soluble Protein ◽  
Amino Acid Profile ◽  
Jack Bean ◽  
Germination Time ◽  
Bean Flour ◽  
Hydrophobic Amino Acids ◽  
Foaming Capacity

Jack bean as a source of vegetable protein had not been popular. Seed germination had been known to improve its nutritional quality, especially protein and amino acid profile. This study determined the effect of germination on the color, beany flavor, protein content, functional properties, and amino acid profile of jack bean flour. A complete randomized design was used for this experiment. Germination was carried out for 0, 24, 48, and 72 hours. The seed (control) and germinated jack bean flours were analyzed for oil absorption, water absorption, emulsifying and foaming capacities, as well as the soluble protein content to determine the best germination time. Furthermore, the amino acid profile of the jack bean flour produced from the best germination time was analyzed. The results of this study indicated that the total and soluble protein of the seed and germinated jack bean seeds for 0, 24, 48, 60, and 72 hours were 23.30 and 5.95; 22.61 and 7.61; 21.18 and 10.68; 23.26 and 10.22; 23.98 and 10.81%, respectively. Germination of jack bean improved the functional properties. A germination time of 72 hours increased the oil capacity, water absorption capacity, foaming capacity and decreased the emulsion capacity significantly. The hydrophilic and hydrophobic amino acids of the germinated jack bean flour increased to 3.21 and 2.12% of the seed flour, respectively. The increase of the foaming capacity was related to the increase in hydrophobic amino acids of germinated jack bean flour compared to seed flours, that were glycine 1.23 and 1.01; alanine 1.29 and 1.01; valine 1.16 and 1.00; leucine 1.84 and 1.09%, respectively. Germination of jack bean for 72 hours increased significantly the essential amino acids, namely: leucine, lysine, and valine.

Sign in / Sign up

Export Citation Format

Share Document