Vibrational Analysis of Amino Acids and Short Peptides in Hydrated Media. VIII. Amino Acids with Aromatic Side Chains:l-Phenylalanine,l-Tyrosine, andl-Tryptophan

2010 ◽  
Vol 114 (46) ◽  
pp. 15319-15330 ◽  
Author(s):  
Belén Hernández ◽  
Fernando Pflüger ◽  
Alain Adenier ◽  
Sergei G. Kruglik ◽  
Mahmoud Ghomi
Keyword(s):  
Amino Acids ◽  
Vibrational Analysis ◽  
Short Peptides

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

Vibrational Analysis of Amino Acids and Short Peptides in Hydrated Media. 3. Successive KL Repeats Induce Highly Stable β-Strands Capable of Forming Non-H-Bonded Aggregates

2008 ◽  
Vol 112 (4) ◽  
pp. 1282-1289 ◽  
Author(s):  
Guy Guiffo-Soh ◽  
Belén Hernández ◽  
Yves-Marie Coïc ◽  
Fatima-Zohra Boukhalfa-Heniche ◽  
Giulia Fadda ◽  
...  
Keyword(s):  
Amino Acids ◽  
Vibrational Analysis ◽  
Short Peptides

Vibrational Analysis of Amino Acids and Short Peptides in Hydrated Media. II. Role of KLLL Repeats To Induce Helical Conformations in Minimalist LK-Peptides

2007 ◽  
Vol 111 (43) ◽  
pp. 12563-12572 ◽  
Author(s):  
Guy Guiffo-Soh ◽  
Belén Hernández ◽  
Yves-Marie Coïc ◽  
Fatima-Zohra Boukhalfa-Heniche ◽  
Mahmoud Ghomi
Keyword(s):  
Amino Acids ◽  
Vibrational Analysis ◽  
Short Peptides

Vibrational Analysis of Amino Acids and Short Peptides in Hydrated Media. I. L-glycine and L-leucine

2007 ◽  
Vol 111 (6) ◽  
pp. 1470-1477 ◽  
Author(s):  
Najoua Derbel ◽  
Belén Hernández ◽  
Fernando Pflüger ◽  
Jean Liquier ◽  
Frédéric Geinguenaud ◽  
...  
Keyword(s):  
Amino Acids ◽  
Vibrational Analysis ◽  
Short Peptides

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.

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