N-Terminus and Lysine Side Chain pKa Values of Melittin in Aqueous Solutions and Micellar Dispersions Measured by 15N NMR

Biochemistry ◽  
1995 ◽  
Vol 34 (40) ◽  
pp. 13196-13202 ◽  
Author(s):  
Lingyang Zhu ◽  
Marvin D. Kemple ◽  
Peng Yuan ◽  
Franklyn G. Prendergast
Keyword(s):  
Aqueous Solutions ◽  
Side Chain ◽  
15N Nmr ◽  
Pka Values ◽  
Lysine Side Chain ◽  
N Terminus

Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear1H−15N NMR Spectroscopy

2011 ◽  
Vol 133 (4) ◽  
pp. 909-919 ◽  
Author(s):  
Alexandre Esadze ◽  
Da-Wei Li ◽  
Tianzhi Wang ◽  
Rafael Brüschweiler ◽  
Junji Iwahara
Keyword(s):  
Nmr Spectroscopy ◽  
Side Chain ◽  
15N Nmr ◽  
Amino Groups ◽  
Lysine Side Chain ◽  
15N Nmr Spectroscopy

Catalytic activity of CuGHK peptide-based porous material

2021 ◽  
Author(s):  
Francisco G. Cirujano ◽  
Nuria Martin ◽  
Neyvis Almora-Barrios ◽  
Carlos Martí-Gastaldo
Keyword(s):  
Catalytic Activity ◽  
Porous Material ◽  
Active Sites ◽  
Room Temperature ◽  
Side Chain ◽  
Periodic Distribution ◽  
Lysine Side Chain ◽  
One Step

Room temperature one-step synthesis of the peptide-based porous material with a periodic distribution of pockets decorated with lysine side chain active sites behaves as a heterogeneous organocatalyst. The pockets are...

Covalent layer-by-layer thin films with charge-transfer chromophores: side chain engineering for efficient Ag+ ion recognition in aqueous solutions

Soft Matter ◽  
2018 ◽  
Vol 14 (44) ◽  
pp. 9055-9060 ◽  
Author(s):  
Hiroyuki Fujita ◽  
Tsuyoshi Michinobu
Keyword(s):  
Thin Films ◽  
Charge Transfer ◽  
Aqueous Solutions ◽  
Side Chain ◽  
Layer By Layer ◽  
Ion Recognition ◽  
Precursor Polymers

Covalent layer-by-layer films, fabricated by [2+2] cycloaddition–retroelectrocyclization, show different Ag+ ion recognition behaviors due to the side-chain groups of precursor polymers.

Azoverdin -an Isopyoverdin

1996 ◽  
Vol 51 (11-12) ◽  
pp. 772-780 ◽  
Author(s):  
R Michalke ◽  
K Taraz ◽  
H Budzikiewiez
Keyword(s):  
Carboxylic Acid ◽  
Succinic Acid ◽  
Peptide Chain ◽  
Side Chain ◽  
Carboxyl Group ◽  
Amino Group ◽  
Present Evidence ◽  
N Terminus

For azoverdin, the siderophore of Azomonas macrocytogenes ATCC 12334, a pyoverdintype structure has been suggested. We now present evidence that it is actually an isopyoverdin. Also the sequence of the peptide chain has to be revised. Azoverdin comprises, therefore, the chromophore (3S)-5-amino-1,2-dihydro-8,9-dihydroxy-3H -pyrimido[1,2a]quinoline- 3-carboxylic acid whose amino group is bound to a succinamide residue while the carboxyl group is attached to the N -terminus of L-Hse-[2-(R-1-amino-3-hydroxypropyl)-3,4,5,6- tetrahydropyrimidine-65-carboxylic acid]-N5-acetyl-N5,-hydroxy-ᴅ-Orn-ᴅ-Ser-N5-acetyl-N5- hydroxy-ʟ-Orn. In addition to azoverdin congeners with succinic acid (azoverdin A ) and with ʟ-Glu (azoverdin G ), resp., instead of the succinamide side chain could be isolated.

Thermodynamic properties of peptide solutions. The relative partial molar enthalpies of aqueous solutions of glycylglycylglycine, glycylglycylalanine and alanylglycylglycine

1983 ◽  
Vol 36 (9) ◽  
pp. 1813 ◽  
Author(s):  
MK Kumaran ◽  
ID Watson ◽  
GR Hedwig
Keyword(s):  
Thermodynamic Properties ◽  
Aqueous Solutions ◽  
Side Chain ◽  
Enthalpies Of Dilution ◽  
Flow Microcalorimetry ◽  
Water Side ◽  
Partial Molar Enthalpies

The enthalpies of dilution at 298 K of aqueous solutions of the tripeptides glycylglycylglycine, glycylglycylalanine and alanylglycylglycine have been determined by flow microcalorimetry. From these data the partial molar enthalpies of the solvent in the solutions have been calculated. The results indicate that water side-chain interactions make an important contribution to the solvation of peptides.

L-Lysine sulphate, C6H16N2O22+.SO42−: a novel conformation of the L-lysine side chain

1983 ◽  
Vol 39 (2) ◽  
pp. 281-283 ◽  
Author(s):  
S. Capasso ◽  
C. A. Mattia ◽  
L. Mazzarella ◽  
A. Zagari
Keyword(s):  
Side Chain ◽  
Lysine Side Chain

scholarly journals Chemical nature and sequence of alamethicin

1976 ◽  
Vol 153 (2) ◽  
pp. 181-190 ◽  
Author(s):  
D R Martin ◽  
R J P Williams
Keyword(s):  
Glutamic Acid ◽  
Chemical Nature ◽  
Chemical Compounds ◽  
Amide Bond ◽  
Side Chain ◽  
Partial Hydrolysis ◽  
Spectroscopy Study ◽  
N Terminus ◽  
Acetyl Group ◽  
New Formula

An n.m.r. spectroscopy study of pure alamethicin shows it to be a linear polypeptide of 19 residues. The N-terminus is blocked by an acetyl group, and the eighteenth residue, glutamic acid, is linked by an amide bond on its side chain to phenylalaninol (Fig. 6). The new formula is confirmed by a comparison between pure chemical compounds and the products of partial hydrolysis.

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