Role of aromatic amino acids in protein-nucleic acid recognition

Biopolymers ◽  
2007 ◽  
Vol 85 (5-6) ◽  
pp. 456-470 ◽  
Author(s):  
Christopher M. Baker ◽  
Guy H. Grant
Keyword(s):  
Amino Acids ◽  
Nucleic Acid ◽  
Aromatic Amino Acids ◽  
Protein Nucleic Acid

Chain Elongation of Aromatic Amino Acids: the Role of 2-Benzylmalic Acid in the Biosynthesis of a C6C4 Amino Acid and a C6C3 Mustard Oil Glucoside

1974 ◽  
Vol 52 (10) ◽  
pp. 916-921 ◽  
Author(s):  
D. Dörnemann ◽  
W. Löffelhardt ◽  
H. Kindl
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aromatic Amino Acids ◽  
Chain Elongation ◽  
Mustard Oil ◽  
Barbarea Vulgaris ◽  
Nasturtium Officinale ◽  
A Chain ◽  
Phenylbutyric Acid

A chemical synthesis of specifically 14C-labelled 2-benzylmalic acid, hitherto unknown, was developed. 4-Phenylacetoacetate obtained by condensation of phenylacetyl chloride-1-14C with ethyl acetoacetate yielded 2-benzylmalic acid-2-14C after cyanohydrin reaction and hydrolysis.2-Benzylmalic acid-2-14C, administered to shoots of Nasturtium officinale and Barbarea vulgaris, was shown to be an efficient precursor of the aglucone moiety of the mustard oil glucoside gluconasturtiin. The incorporation of radioactivity agreed well with the values reported for incorporation of 3-benzylmalic acid, but was considerably higher than that obtained after application of L-phenylalanine-U-14C. A conversion of 2-benzylmalic acid into 3-benzylmalic acid and 2-amino-4-phenylbutyric acid could also be demonstrated. These findings provide the final evidence for a chain-lengthening mechanism leading to homologous amino acids as proposed by Underbill and Wetter in 1966.

Ultraviolet Resonance Raman Spectra of Escherichia Coli with 222.5–251.0 nm Pulsed Laser Excitation

1988 ◽  
Vol 42 (5) ◽  
pp. 782-788 ◽  
Author(s):  
K. A. Britton ◽  
R. A. Dalterio ◽  
W. H. Nelson ◽  
D. Britt ◽  
J. F. Sperry
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Nucleic Acid ◽  
Raman Spectra ◽  
Resonance Raman ◽  
Aromatic Amino Acids ◽  
Selective Excitation ◽  
Exciting Wavelength ◽  
Resonance Raman Spectra ◽  
Ultraviolet Resonance Raman

Resonance Raman spectra of the gram-negative organism, Escherichia coli, have been obtained with 222.5-, 230.6-, and 251.0-nm excitation, and the results have been compared with those reported earlier for 242.4-nm excitation. Major changes in bacterial spectra have been observed with changes in exciting wavelength. The origins of the major peaks in each spectrum have been explained primarily in terms of contributions of nucleic acid bases and aromatic amino acids. As an aid in making assignments, spectra of aromatic amino acids, nucleosides, and mixtures of the two have been obtained at each wavelength used to excite bacterial spectra. Background fluorescence has been observed to be negligible below 251 nm. Selective excitation of bacterial nucleic acid and protein components has been done with ease. Results suggest that an extension of the exciting wavelength range to 190–220 nm will allow the selective excitation of additional cell components.

Role of Acidic and Aromatic Amino Acids inRhodobacter CapsulatusCytochromec1. A Site-Directed Mutagenesis Study†

Biochemistry ◽  
2003 ◽  
Vol 42 (29) ◽  
pp. 8818-8830 ◽  
Author(s):  
Jun Li ◽  
Artur Osyczka ◽  
Richard C. Conover ◽  
Michael K. Johnson ◽  
Hong Qin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
A Site ◽  
Mutagenesis Study

scholarly journals Dissecting the role of protein-protein and protein-nucleic acid interactions in MS2 bacteriophage stability

FEBS Journal ◽  
2006 ◽  
Vol 273 (7) ◽  
pp. 1463-1475 ◽  
Author(s):  
Sheila M. B. Lima ◽  
Ana Carolina Q Vaz ◽  
Theo L. F. Souza ◽  
David S. Peabody ◽  
Jerson L. Silva ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Ms2 Bacteriophage ◽  
Protein Nucleic Acid ◽  
Nucleic Acid Interactions

Order controls disordered droplets: structure-function relationships in C9orf72-derived poly(PR)

2021 ◽  
Author(s):  
Kohsuke Kanekura ◽  
Yuhei Hayamizu ◽  
Masahiko Kuroda
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids ◽  
Polar Amino Acid ◽  
Repeat Proteins ◽  
Intron 1 ◽  
Lateral Sclerosis ◽  
Ran Translation ◽  
Dipeptide Repeat ◽  
Positively Charged

Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) have been thought as two distinct neurodegenerative diseases. However, recent genetic screening and careful investigations found the genetic and pathological overlap among these disorders. Hexanucleotide expansions in intron 1 of C9orf72 are a leading cause of familial ALS and familial FTD. These expansions facilitate the repeat-associated non-ATG initiated translation (RAN translation), producing five dipeptide repeat proteins (DRPs), including Arg-rich poly(PR: Pro-Arg) and poly-(GR: Gly-Arg) peptides. Arg is a positively charged, highly polar amino acid that facilitates interactions with anionic molecules such as nucleic acids and acidic amino acids via electrostatic forces and aromatic amino acids via cation-pi interaction, suggesting that Arg-rich DRPs underlie the pathophysiology of ALS via Arg-mediated molecular interactions. Arg-rich DRPs have also been reported to induce neurodegeneration in cellular and animal models via multiple mechanisms; however, it remains unclear why the Arg-rich DRPs exhibit such diverse toxic properties, because not all Arg-rich peptides are toxic. In this mini-review, we discuss the current understanding of the pathophysiology of Arg-rich C9orf72 DRPs and introduce recent findings on the role of Arg distribution as a determinant of the toxicity and its contribution to the pathogenesis of ALS.

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