Adsorption of biomedical coating molecules, amino acids, and short peptides on magnetite (110)

2015 ◽  
Vol 143 (4) ◽  
pp. 044705 ◽  
Author(s):  
Ulrich Aschauer ◽  
Annabella Selloni
Keyword(s):  
Amino Acids ◽  
Short Peptides ◽  
Biomedical Coating

scholarly journals The Glycine- and Proline-Rich Protein AtGPRP3 Negatively Regulates Plant Growth in Arabidopsis

2020 ◽  
Vol 21 (17) ◽  
pp. 6168
Author(s):  
Xiaojing Liu ◽  
Xin Wang ◽  
Xin Yan ◽  
Shaobo Li ◽  
Hui Peng
Keyword(s):  
Amino Acids ◽  
Plant Growth ◽  
Physiological Role ◽  
Short Peptides ◽  
Hydrophobic Domain ◽  
Gfp Fusion Protein ◽  
Repeat Domain ◽  
Arabidopsis Plant ◽  
Proline Rich Protein

Glycine- and proline-rich proteins (GPRPs) comprise a small conserved family that is widely distributed in the plant kingdom. GPRPs are relatively short peptides (<200 amino acids) that contain three typical domains, including an N-terminal XYPP-repeat domain, a middle hydrophobic domain rich in alanine, and a C-terminal HGK-repeat domain. These proteins have been proposed to play fundamental roles in plant growth and environmental adaptation, but their functions remain unknown. In this study, we selected an Arabidopsis GPRP (AtGPRP3) to profile the physiological role of GPRPs. Transcripts of AtGPRP3 could be detected in the whole Arabidopsis plant, but greater amounts were found in the rosette, followed by the cauline. The AtGPRP3::GFP fusion protein was mainly localized in the nucleus. The overexpression and knockout of AtGPRP3, respectively, retarded and accelerated the growth of Arabidopsis seedlings, while the increase in the growth rate of atgprp3 plants was offset by the complementary expression of AtGPRP3. CAT2 and CAT3, but not CAT1, interacted with AtGPRP3 in the nuclei of Arabidopsis protoplasts. The knockout of CAT2 by CRISPR-Cas9 retarded the growth of the Arabidopsis seedlings. Together, our data suggest that AtGPRP3 negatively regulates plant growth, potentially through CAT2 and CAT3.

scholarly journals THE PROPERTIES AND THE ENZYMATIC DEGRADATION OF DESOXYRIBONUCLEOPROTEIN FROM LIVER CELL NUCLEI

1958 ◽  
Vol 41 (3) ◽  
pp. 595-608 ◽  
Author(s):  
Kenneth J. Monty ◽  
Alexander L. Dounce
Keyword(s):  
Amino Acids ◽  
Cell Nucleus ◽  
Liver Cell ◽  
Enzymatic Degradation ◽  
Short Peptides ◽  
Chromosomal Protein ◽  
X Rays ◽  
Cell Nuclei ◽  
Desoxyribonucleic Acid ◽  
Mode Of Attachment

The isolation and properties of a desoxyribonucleoprotein of the rat liver cell nucleus are described. This material consists of DNA (desoxyribonucleic acid) bound to the residual chromosomal protein by what appear to be covalent linkages. Lipide is present, but can be removed by extraction in lipide solvents prior to isolation of the nucleoprotein, without much change in the physical properties of the latter. The nucleoprotein in question forms elastic, recoilable gels in molar saline at pH 7.0 or in water at pH 8.0 to 10.0 or even higher, which are similar to those that can be obtained from whole nuclei. The effects of x-rays, heat, and enzymes on the nucleoprotein are discussed, and the composition of the protein component is investigated. The latter contains an "occult" protein that can be liberated by heating in 0.1 N HCl. A study of the enzymatic degradation of the desoxyribonucleoprotein has been made, with the aim of attempting the isolation of small polynucleotide fragments attached to amino acids or short peptides that might be useful in characterizing the mode of attachment of the desoxyribonucleic acid to the protein in the desoxyribonucleoprotein. Evidence is presented indicating that such products can be isolated through the use of electrophoresis on paper.

Accelerated ripening of Pecorino Umbro cheese

1998 ◽  
Vol 65 (4) ◽  
pp. 631-642 ◽  
Author(s):  
ALDO CORSETTI ◽  
MARCO GOBBETTI ◽  
EMANUELE SMACCHI ◽  
MARIA DE ANGELIS ◽  
JONE ROSSI
Keyword(s):  
Amino Acids ◽  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Free Amino ◽  
Trichloroacetic Acid ◽  
Short Peptides ◽  
Accelerated Ripening ◽  
Total Free Amino Acids ◽  
Biochemical Analyses ◽  
Dipeptidase Activities

We have investigated accelerating the ripening of Pecorino Umbro cheese by adding crude cytoplasmic extract from Pseudomonas fluorescens, non-starter lactic acid bacteria (NSLAB) or cheese slurry. Microbiological and biochemical analyses and sensory evaluation were carried out on control and experimental cheeses over 28 d ripening. In the cheeses containing NSLAB or slurry, counts of mesophilic lactobacilli ranged from log 7·6 at day 1 to ∼log 8·6 cfu/g after 28 d ripening, ∼2 log cycles higher than in the control cheese. All the experimental cheeses contained higher levels than the control of total free amino acids and N soluble at pH 4·6 and in 120 g trichloroacetic acid/l. Compared with the control, higher aminopeptidase and dipeptidase activities were found in the cheeses containing NSLAB and slurry, and especially in those containing the Pseudomonas enzyme. The cheeses containing NSLAB or slurry were characterized by an accumulation of short peptides (Mr<2000) detected by FPLC. Although the cheese containing enzyme had an atypical flavour, the addition of mesophilic lactobacilli reduced from 60 to 28 d the ripening period of Pecorino Umbro cheese, without the appearance of off flavour.

Residual Dipolar Couplings in Short Peptides Reveal Systematic Conformational Preferences of Individual Amino Acids

2006 ◽  
Vol 128 (41) ◽  
pp. 13508-13514 ◽  
Author(s):  
Sonja Alexandra Dames ◽  
Regula Aregger ◽  
Navratna Vajpai ◽  
Pau Bernado ◽  
Martin Blackledge ◽  
...  
Keyword(s):  
Amino Acids ◽  
Residual Dipolar Couplings ◽  
Dipolar Couplings ◽  
Short Peptides ◽  
Conformational Preferences

scholarly journals Large-scale docking predicts that sORF-encoded peptides may function through protein-peptide interactions in Arabidopsis thaliana

2018 ◽  
Author(s):  
Rashmi R. Hazarika ◽  
Nikolina Sostaric ◽  
Yifeng Sun ◽  
Vera van Noort
Keyword(s):  
Amino Acids ◽  
Arabidopsis Thaliana ◽  
Large Scale ◽  
Hydrophobic Interactions ◽  
Peptide Binding ◽  
Coarse Grained ◽  
Short Peptides ◽  
Cofactor Binding ◽  
Starting Point ◽  
Peptide Interactions

AbstractSeveral recent studies indicate that small Open Reading Frames (sORFs) embedded within multiple eukaryotic non-coding RNAs can be translated into bioactive peptides of up to 100 amino acids in size. However, the functional roles of the 607 Stress Induced Peptides (SIPs) previously identified from 189 Transcriptionally Active Regions (TARs) inArabidopsis thalianaremain unclear. To provide a starting point for function annotation of these peptides, we performed a large-scale prediction of peptide binding sites on protein surfaces using and coarse-grained peptide docking. The docked models were subjected to further atomistic refinement and binding energy calculations. A total of 530 peptide-protein pairs were successfully docked. In cases where a peptide encoded by a TAR is predicted to bind at a known ligand or cofactor-binding site within the protein, it can be assumed that the peptide modulates the ligand or cofactor-binding. Moreover, we predict that several peptides bind at protein-protein interfaces, which could therefore regulate the formation of the respective complexes. Protein-peptide binding analysis further revealed that peptides employ both their backbone and side chain atoms when binding to the protein, forming predominantly hydrophobic interactions and hydrogen bonds. In this study, we have generated novel predictions on the potential protein-peptide interactions inA. thaliana, which will help in further experimental validation.Author summaryDue to their small size, short peptides are difficult to find and have been ignored in genome annotations. Only recently, we have realized that these short peptides of less than 100 amino acids may actually play an important role in the cell. Currently, there are no high-throughput methods to find out what the functions of these peptides are in contrast with efforts that exist for ‘normal’proteins. In this work, we try to fill this gap by predicting with which larger proteins, the short peptides might interact to exert their function. We find that many peptides bind to pockets where normally other proteins or molecules bind. We thus think that these peptides that are induced by stress, may regulate protein-protein and protein-molecule binding. We make this information available through our database ARA-PEPs so that individual predictions can be followed up.

Vibrational Analysis of Amino Acids and Short Peptides in Hydrated Media. VI. Amino Acids with Positively Charged Side Chains:l-Lysine andl-Arginine

2010 ◽  
Vol 114 (2) ◽  
pp. 1077-1088 ◽  
Author(s):  
Belén Hernández ◽  
Fernando Pflüger ◽  
Najoua Derbel ◽  
Joël De Coninck ◽  
Mahmoud Ghomi
Keyword(s):  
Amino Acids ◽  
Vibrational Analysis ◽  
Short Peptides ◽  
Positively Charged

scholarly journals Studies on sequencing of peptides from the carboxyl terminus by using the thiocyanate method

1976 ◽  
Vol 157 (2) ◽  
pp. 307-316 ◽  
Author(s):  
M Rangarajan ◽  
A Darbre
Keyword(s):  
Amino Acids ◽  
Freeze Drying ◽  
Solid Phase ◽  
Glass Beads ◽  
Carboxyl Terminus ◽  
Short Peptides ◽  
Free Solution ◽  
Active Ester ◽  
Low Levels ◽  
Modified Polystyrene

We report on our experience in applying the thiocyanate method developed by Stark (1968) (Biochemistry 7, 1796-1807) to the sequencing of short peptides from the carboxyl end in free solution. Yields fell to very low levels after three cycles of degradation. The method was time-consuming because of the filtration and freeze-drying stages involved. To overcome these problems, peptides were attached to modified polystyrene polymers for sequential degradation in the solid phase, and a maximum of six amino acids was determined. Also, ribonuclease was attached to active-ester glass beads and sequential degradation was carried out to determine six amino acids at the C-terminal end of this protein.

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