The crystal structure of<scp>l</scp>-arginine hydrochloride*

Μazumdar, S. Κ.; Venkatesan, Κ.; Mez, Hans‐Christian; Donohue, Jerry

doi:10.1524/zkri.1969.130.1-6.328

Cited by 27 publications

(11 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Only resolved 13 C signals were used to report the T 2 values. Arginine hydrochloride shows two peaks for each 13 C site due to two inequivalent molecules in the asymmetric unit cell 56,57 . Representative T 2 decays are shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Line Widths and Line Shapes

Hong

2011

J. Phys. Chem. B

View full text Add to dashboard Cite

A challenge in the application of solid-state NMR spectroscopy to membrane peptides and proteins is the relatively broad linewidths compared to solution NMR spectra. To understand the linewidth contributions to membrane protein NMR spectra, we have measured the inhomogeneous and homogeneous linewidths of several well-studied membrane peptides under immobilized conditions. 13C T2 relaxation times of uniformly 13C-labeled residues show that the homogeneous linewidths of the peptides are comparable to those of crystalline model compounds under identical 1H decoupling and magic-angle-spinning conditions, indicating that the homogeneous linewidths are determined by conformation-independent factors, including residual dipolar coupling, J coupling and intrinsic T2 relaxation. However, the membrane peptides exhibit larger apparent linewidths than the crystalline compounds, indicating conformational disorder. A cationic cell-penetrating peptide, the human immunodeficiency virus TAT, exhibits the largest apparent linewidths, which are about 5-fold larger than the homogeneous linewidths, while the transmembrane helix of the influenza M2 peptide and the β-hairpin antimicrobial peptide PG-1 show moderately larger apparent linewidths than the crystalline compounds. These results are consistent with the random coil nature of the TAT peptide, which contrasts with the intramolecularly hydrogen-bonded M2 and PG-1. Cross peak lineshapes of 2D double-quantum correlation spectra show that the conformational disorder can occur at the residue level and can result from three origins: lipid-peptide interaction, intrinsic conformational disorder encoded in the amino acid sequence, and sidechain rotameric averaging. A particularly important lipid-peptide interaction for cationic membrane peptides is guanidinium-phosphate ion pair interaction. Thus, NMR linewidths and lineshapes are useful for understanding the conformational disorder of membrane peptides and proteins.

show abstract

Section: Resultsmentioning

confidence: 99%

Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Line Widths and Line Shapes

Hong

2011

J. Phys. Chem. B

View full text Add to dashboard Cite

show abstract

“…In this paper, we report the structure of a triclinic polymorph of l-argininium chloride, (I). An earlier structure determination of (I) was carried out by visual methods in the monoclinic space group P2 1 (Mazumdar et al, 1969). The transformation (102/100/010) of the present data to the monoclinic setting using the LEPAGE routine in PLATON (Spek, 1999) resulted in a high R int (0.37) value.…”

mentioning

confidence: 94%

“…ÁCl À , crystallizes in the triclinic system with two crystallographically independent argininium residues and two chloride ions in the P1 unit cell. In an earlier study, the structure of l-arginine chloride [Mazumdar et al (1969). Z. Kristallogr.…”

mentioning

confidence: 99%

A triclinic polymorph ofL-argininium chloride

Sridhar

Srinivasan²,

Dalhus

et al. 2002

Acta Cryst E

View full text Add to dashboard Cite

The title compound, C6H15N4O2+·Cl−, crystallizes in the triclinic system with two crystallographically independent argininium residues and two chloride ions in the P1 unit cell. In an earlier study, the structure of l‐arginine chloride [Mazumdar et al. (1969). Z. Kristallogr. 130, 328–339] was determined in the monoclinic space group P21. In our work, the side‐chain conformation has an all‐trans form in one of the residues, whereas in the other residue, it is in the gauche I‐trans‐trans‐trans form. All the N atoms, carboxylate groups and chloride ions are involved in a hydrogen‐bonding network.

show abstract

“…Based on the result of LAHCL crystal size obtained from experiments, i.e., 61 × 287 × 61 μm, the volume occupied by one crystal was calculated to be ∼ 1.07 × 10 −12 m 3 which is equal to ∼ 1.45 × 10 −6 g with a crystal density of 1.355 × 10 6 g m −3 10. Also, it is well‐known that four LAHCL molecules are in the unit cell of dimensions, a = 5.33 Å, b = 9.46 Å, c = 20.07 Å, β = 90°30′, and V = 1011.9 Å 3 8, 11. To simplify the calculations, the cell length was set at 10.04 Å to establish V = 1011.9 Å 3 .…”

Section: Resultsmentioning

confidence: 99%

Effect of Specific Amino Acids on Controlling Crystal Pseudopolymorphism of L‐Arginine Hydrochloride

Shimizu

Yoshiura²,

Nagano

et al. 2014

Chem Eng & Technol

View full text Add to dashboard Cite

The effect of a small amount of amino acid additives on the pseudopolymorphism of L-arginine hydrochloride (LAHCL) in aqueous solution is reported. Results confirm that L-alanine (L-Ala) has a stabilizing effect on the crystals of the anhydrate form of LAHCL at low temperature. Intriguingly, the stabilizing effect was observed even when L-Ala was added after a large amount of LAHCL had formed. In contrast, no stabilizing effect with D-Ala could be stated, suggesting that the stereochemistry of the additives is an important factor. In addition to the stereochemistry, also the length and bulkiness of the alkyl side-chain of the amino acids were found to be significant factors. Based on these results, a mechanism is proposed for stabilization of anhydrate LAHCL crystals by amino acid additives.

show abstract

The crystal structure ofl-arginine hydrochloride*

Cited by 27 publications

References 0 publications

Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Line Widths and Line Shapes

Conformational Disorder of Membrane Peptides Investigated from Solid-State NMR Line Widths and Line Shapes

A triclinic polymorph ofL-argininium chloride

Effect of Specific Amino Acids on Controlling Crystal Pseudopolymorphism of L‐Arginine Hydrochloride

Contact Info

Product

Resources

About