N.M.R. studies of myelin basic protein. VI. Proton spectra in aqueous solutions of proteins from mammalian and avian species

1982 ◽  
Vol 35 (10) ◽  
pp. 1979 ◽  
Author(s):  
GL Mendz ◽  
WJ Moore ◽  
PR Carnegie
Keyword(s):  
Aqueous Solution ◽  
Primary Structure ◽  
Chemical Shifts ◽  
Side Chains ◽  
Amino Acid Residues ◽  
Difference Spectra ◽  
Effects Of Ph ◽  
Central Nervous Systems ◽  
Species Comparisons ◽  
Nuclear Overhauser

Myelin basic proteins from human, cow, pig, rabbit and chicken central nervous systems were studied in aqueous solution by proton n.m.r. at 400 MHz. Species comparisons and other techniques led to the assignment of resonances of 23 specific amino acid residues in the primary structure. Resonances from side chains of polar amino acids adjacent to aspartic residues could be assigned by anomalous effects of pH on the chemical shifts. The pK values of histidine side chains all fall in the range 6.0-6.9, and four specific histidine residues were assigned. The conformation of the protein in aqueous solution is that of an extended non-random polypeptide chain with regions of localized structure. Nuclear Overhauser difference spectra showed that a reverse turn similar to that previously suggested for an encephalitogenic nonapeptide isolated from the protein (guinea pig determinant) occurs also in the protein itself, thus supporting the concept of special low-energy conformations responsible for biological activity. Upfield chemical shifts of some side chain methyl groups from the central region of the primary structure suggest ring-current shifts due to higher-order structuring.

scholarly journals The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues

1975 ◽  
Vol 149 (3) ◽  
pp. 497-506 ◽  
Author(s):  
S Doonan ◽  
H J Doonan ◽  
R Hanford ◽  
C A Vernon ◽  
J M Walker ◽  
...  
Keyword(s):  
Primary Structure ◽  
Aspartate Aminotransferase ◽  
The Other ◽  
British Library ◽  
Side Chains ◽  
Amino Acid Residues ◽  
Main Paper ◽  
Lysine Residues ◽  
Arginine Residues ◽  
Complete Primary Structure

Carboxymethylated aspartate aminotransferase was digested with a proteinase claimed to be specific for lysine residues. Complete cleavage occurred at 12 of the 19 lysine residues in the protein, but at the remaining seven residues cleavage was either restricted or absent. In addition, cleavage was observed at three of the 26 arginine residues. These results are discussed with reference to the amino acid residues adjacent to points of complete or restricted cleavage. The complete primary structure of aspartate aminotransferase, based on these and other studies, is given. Evidence for the assignment of some acid and amide side chains has been deposited as Supplementary Publication SUP 50050 (11 pp.) at the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975) 145, 5. The evidence for the assignment of residue 366 was less conclusive than for the other acid and amide side chains and is, therefore, given in the main paper.

An NMR study of the Lycopodium alkaloids, annotinine and annotine: verification of the annotine structure

1989 ◽  
Vol 67 (11) ◽  
pp. 1765-1773 ◽  
Author(s):  
Donald W. Hughes ◽  
Robert V. Gerard ◽  
David B. MacLean
Keyword(s):  
Chemical Shifts ◽  
Structural Data ◽  
Double Quantum ◽  
Difference Spectra ◽  
Nmr Data ◽  
Nmr Study ◽  
Lycopodium Alkaloids ◽  
Phase Sensitive ◽  
Nuclear Overhauser ◽  
C Nmr

The Lycopodium alkaloids, annotinine and annotine, were examined by 1H and 13C NMR spectroscopy. Proton spectra were assigned by the application of double-quantum filtered phase-sensitive COSY and nuclear Overhauser enhancement difference spectra. These and other data confirmed the structure previously assigned to annotine. The 13C chemical shifts were consistent with the structural data derived from the proton spectra. The NMR data showed a good correlation with structures determined from molecular mechanics (MMX) calculations. Keywords: Lycopodium alkaloids 1H and 13C NMR, annotinine, annotine, structure of Lycopodium alkaloids, NMR alkaloids.

The stereochemistry of some 7-hydroxyindene dimers: applications of 1H nuclear magnetic resonance relaxation pathway analysis

1985 ◽  
Vol 63 (8) ◽  
pp. 2332-2338 ◽  
Author(s):  
Walter J. Chazin ◽  
Lawrence D. Colebrook ◽  
Brian R. Davis ◽  
I. Ross N. McCormick ◽  
Stephen J. Johnson
Keyword(s):  
Nuclear Overhauser Effect ◽  
Chemical Shifts ◽  
Lattice Relaxation ◽  
Spin Lattice Relaxation ◽  
Relaxation Rates ◽  
Difference Spectra ◽  
Spin Lattice ◽  
Relative Stereochemistry ◽  
Effect Difference ◽  
Nuclear Overhauser

1H spin-lattice relaxation rates and nuclear Overhauser effect difference spectra have been measured (at 400 MHz) for six dimers derived from methyl-substituted 7-hydroxyindenes. Used in combination, these measurements identify the relaxation pathways available to all of the protons in the molecules. Analysis of these pathways has permitted assignment of all chemical shifts, and identification of the relative stereochemistry at all chiral centres.

The isolation, structure, and stereochemistry of traversiadiene. The precursor hydrocarbon of traversianal biosynthesis

1989 ◽  
Vol 67 (8) ◽  
pp. 1302-1304 ◽  
Author(s):  
Albert Stoessl ◽  
G. L. Rock ◽  
J. B. Stothers
Keyword(s):  
Magnetic Resonance ◽  
Biosynthetic Pathway ◽  
Nuclear Overhauser Effect ◽  
Difference Spectra ◽  
Heteronuclear Correlation ◽  
Magnetic Resonance Studies ◽  
Overhauser Effect ◽  
Effect Difference ◽  
Nuclear Overhauser ◽  
Magnetic Resonance Spectra

A tricyclic diene, traversiadiene, isolated from cultures of Cercosporatraversiana has been shown to have the structure and stereochemistry of the previously postulated hydrocarbon intermediate on the biosynthetic pathway to traversianal (1). Detailed:1H and 13C magnetic resonance studies, including homo- and heteronuclear correlation spectra, led to the gross structure, and the stereochemistry was established through a series of nuclear Overhauser effect difference spectra. Keywords: diterpene, traversiadiene, 1H and 13C magnetic resonance spectra.

On the Origins of Core−Electron Chemical Shifts of Small Biomolecules in Aqueous Solution: Insights from Photoemission andab InitioCalculations of Glycineaq

2011 ◽  
Vol 133 (9) ◽  
pp. 3120-3130 ◽  
Author(s):  
Niklas Ottosson ◽  
Knut J. Børve ◽  
Daniel Spångberg ◽  
Henrik Bergersen ◽  
Leif J. Sæthre ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Chemical Shifts ◽  
Core Electron ◽  
Small Biomolecules

scholarly journals The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastase

1973 ◽  
Vol 133 (4) ◽  
pp. 805-819 ◽  
Author(s):  
Francesco Bossa ◽  
Donatella Barra ◽  
Massimo Carloni ◽  
Paolo Fasella ◽  
Francesca Riva ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Primary Structure ◽  
Aspartate Aminotransferase ◽  
Heart Muscle ◽  
Science And Technology ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Lending Library

Peptides produced by thermolytic digestion of aminoethylated aspartate aminotransferase and of the oxidized enzyme were isolated and their amino acid sequences determined. Digestion by elastase of the carboxymethylated enzyme gave peptides representing approximately 40% of the primary structure. Fragments from these digests overlapped with previously reported sequences of peptides obtained by peptic and tryptic digestion (Doonan et al., 1972), giving ten composite peptides containing 395 amino acid residues. The amino acid composition of these composite peptides agrees well with that of the intact enzyme. Confirmatory results for some of the present data have been deposited as Supplementary Publication 50018 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.

scholarly journals Primary Structure Analysis of Antifungal Peptides from Cultivated and Wild Cereals

Plants ◽  
2018 ◽  
Vol 7 (3) ◽  
pp. 74 ◽  
Author(s):  
Eugene Rogozhin ◽  
Dmitry Ryazantsev ◽  
Alexey Smirnov ◽  
Sergey Zavriev
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Antifungal Activity ◽  
Antimicrobial Peptides ◽  
Structure Analysis ◽  
Primary Structure ◽  
Biologically Active ◽  
Amino Acid Residues ◽  
Wild Cereals ◽  
Determining Factor

Cereal-derived bioactive peptides with antimicrobial activity have been poorly explored compared to those from dicotyledonous plants. Furthermore, there are a few reports addressing the structural differences between antimicrobial peptides (AMPs) from cultivated and wild cereals, which may shed light on significant varieties in the range and level of their antimicrobial activity. We performed a primary structure analysis of some antimicrobial peptides from wild and cultivated cereals to find out the features that are associated with the much higher antimicrobial resistance characteristic of wild plants. In this review, we identified and analyzed the main parameters determining significant antifungal activity. They relate to a high variability level in the sequences of C-terminal fragments and a high content of hydrophobic amino acid residues in the biologically active defensins in wild cereals, in contrast to AMPs from cultivated forms that usually exhibit weak, if any, activity. We analyzed the similarity of various physicochemical parameters between thionins and defensins. The presence of a high divergence on a fixed part of any polypeptide that is close to defensins could be a determining factor. For all of the currently known hevein-like peptides of cereals, we can say that the determining factor in this regard is the structure of the chitin-binding domain, and in particular, amino acid residues that are not directly involved in intermolecular interaction with chitin. The analysis of amino acid sequences of alpha-hairpinins (hairpin-like peptides) demonstrated much higher antifungal activity and more specificity of the peptides from wild cereals compared with those from wheat and corn, which may be associated with the presence of a mini cluster of positively charged amino acid residues. In addition, at least one hydrophobic residue may be responsible for binding to the components of fungal cell membranes.

Model of a folded polypeptide chain

1950 ◽  
Vol 137 (886) ◽  
pp. 79-79
Keyword(s):  
Amino Acid ◽  
Polypeptide Chain ◽  
Molecular Model ◽  
Polymer Chains ◽  
Side Chains ◽  
Amino Acid Residues ◽  
Infra Red ◽  
New Type ◽  
Folded Proteins ◽  
Red Radiation

The models on view in the ante-room show a way of folding a polypeptide chain which is consistent with some observations we have recently made with polarized infra-red radiation (Ambrose & Hanby 1949; Ambrose, Elliott & Temple 1949). The α -folded proteins, keratin, myosin and tropomyosin, have been found when oriented to show greater absorption of the N-H frequency when the electric vector of the absorbed radiation is in the direction of the fibre axis, hence the N-H bond must be preferentially oriented in this direction. A study of models has suggested that the only likely folding of the polypeptide chain consistent with this fact involves a seven-membered ring containing two amino-acid residues; the ring is completed by hydrogen bonds: A new type of atomic model which has been developed in our laboratories has been used. The scale is 0·8 in. to the Angstrom unit. The valency links, while allowing free rotation about single co-valent bonds, also allow some distortion of the bond angles when strains occur but are strong enough to allow long polymer chains to be built. The molecular model exhibited shows twenty-four amino-acid residues, with side chains on one side of the back-bone, representative of those occurring in myosin; the side chains on the other side have been removed for clearness and their positions indicated by single carbon atoms.

Sign in / Sign up

Export Citation Format

Share Document