Conformational Properties of the Amino Acid Residues L-Cysteine, L-Serine and L-Cystine.

Görbitz, Carl Henrik; Yang, Xiaomin; Sauerwein, Björn; Schuster, Gary B.; Nielsen, M.; Lehmann, Martin; Tokii, Tadashi

doi:10.3891/acta.chem.scand.44-0584

Cited by 14 publications

(7 citation statements)

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“…The cysteine molecule is in its zwitterionic tautomer. In principle, the N1-C2-C1-S1 torsion angle (1) can adopt values of ca 60 (gauche-+ or g + ), À60 (g À ) and 180 (trans or t), although in small molecules there is a strong preference for the g + conformation (Gö rbitz, 1990). In l-cysteine-I, 1 = 65.32 (13) (g + , Fig.…”

Section: Resultsmentioning

confidence: 99%

High-pressure polymorphism in L-cysteine: the crystal structures of L-cysteine-III and L-cysteine-IV

Moggach

Allan

Clark

et al. 2006

Acta Crystallogr Sect B

120

106

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The crystal structure of the orthorhombic phase of L-cysteine (hereafter L-cysteine-I) consists of chains of molecules linked via NH...O hydrogen bonds. The chains are linked into a layer by other NH...O hydrogen bonds, forming R4(4)(16) ring motifs. The layers are linked by further NH...O and disordered SH...S/SH...O interactions. The main effects of compression to 1.8 GPa are to contract voids in the middle of the R4(4)(16) rings and to reduce S...S distances from 3.8457 (10) to 3.450 (4) angstroms. The latter is at the lower limit for S...S distances and we suggest that strain about the S atom is responsible for the formation of a new phase of L-cysteine, L-cysteine-III, above 1.8 GPa. The phase transition is accompanied by a change in the NCCS torsion angle from ca 60 to ca -60 degrees and small positional displacements, but with no major changes in the orientations of the molecules. The structure of L-cysteine-III contains similar R-type ring motifs to L-cysteine-I, but there are no S...S contacts within 3.6 angstroms. L-Cysteine-III was found to be stable to at least 4.2 GPa. On decompression to 1.7 GPa, another single-crystal to single-crystal phase transition formed another previously uncharacterized phase, L-cysteine-IV. This phase is not observed on increasing pressure. The structure consists of two crystallographically independent cysteine molecules in the same conformations as those found in L-cysteine-I and L-cysteine-III. The structure separates into zones with are alternately phase I-like and phase III-like. L-Cysteine-IV can therefore be thought of as an unusual example of an intermediate phase. Further decompression to ambient pressure generates L-cysteine-I.

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Section: Resultsmentioning

confidence: 99%

High-pressure polymorphism in L-cysteine: the crystal structures of L-cysteine-III and L-cysteine-IV

Moggach

Allan

Clark

et al. 2006

Acta Crystallogr Sect B

120

106

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“…Görbitz [40] has shown that crystal structures of cysteine and cysteinyl-containing small molecules reveal predominantly gauche + conformations. In addition, MacArthur and Thornton [41] have analyzed the conformations of protein side chains and have shown that cysteinyl groups display predominantly gauche conformations.…”

Section: Rotamersmentioning

confidence: 99%

The solid-state molecular structure of the S-nitroso derivative of l-cysteine ethyl ester hydrochloride

Khan

Lee

et al. 2005

Nitric Oxide

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Nitrosation of protein sulfhydryl groups to form thionitrites (S-nitrosothiols) has been reported to be important in the biochemistry of nitric oxide. Such S-nitrosation of protein thiol residues has been shown to alter the function of some proteins. In this brief communication, we report the X-ray crystal structure of S-nitroso-L-cysteine ethyl ester hydrochloride. Two rotamers with respect to the NCCS moiety are present in the crystal: the major rotamer is in the gauche+ conformation, and the minor rotamer is in the rare anti (trans, antiperiplanar) conformation for a cysteinyl compound. Importantly, the CSNO groups for both rotamers are in the syn (cis, synperiplanar) form. To the best of our knowledge, this is the first reported high-resolution solid-state structure of an S-nitroso derivative of a cysteine or cysteinyl-containing compound.

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“…[3][4][5][6] Serine is one of the 20 naturally occurring amino acids and contributes significantly to the structures of proteins since it readily forms several hydrogen bonds with other protein side groups. [7,8] Recently, new attention has been paid to serine from both the experimental and theoretical sides. Gronert and O'Hair had reported probably the most complete theoretical investigation of the potential energy surface of a neutral serine monomer.…”

Section: Introductionmentioning

confidence: 99%

Conformations of Serine in Aqueous Solutions as Revealed by Vibrational Circular Dichroism

et al. 2012

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Vibrational circular dichroism (VCD) spectroscopy is utilized to reveal the detailed conformational distributions of the dominant serine species in aqueous solutions under three representative pH conditions of 1.0, 5.7, and 13.0, together with vibrational absorption (VA) spectroscopy, density functional theory (DFT), and molecular dynamics simulation. The experimental VA and VCD spectra of serine in H(2)O and D(2)O in the fingerprint region under three pH values are obtained. DFT calculations at the B3LYP/6-311++G(d,p) level are carried out for the protonated, zwitterionic, and deprotonated serine species. The lowest-energy conformers of all three species are identified and their corresponding VA and VCD spectra simulated. A comparison between the gas-phase simulations and the experimental VA and VCD spectra suggests that one or two of the most stable conformers of each species contribute predominantly to the observed data, although some discrepancies are noted. To account for the solvent effects, both the polarizable continuum model and the explicit solvation model are considered. Hydrogen-bonded protonated, zwitterionic, and deprotonated serine-(water)(6) clusters are constructed based on radial distribution function analyses and molecular dynamics snapshots. Geometry optimization and VA and VCD simulations are performed for these clusters at the B3LYP/6-311++G(d,p) level. Inclusion of the explicit water molecules is found to improve the agreement between theory and experiment noticeably in all three cases, thus enabling conclusive conformational distribution analyses of serine in aqueous solutions directly.

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Conformational Properties of the Amino Acid Residues L-Cysteine, L-Serine and L-Cystine.

Cited by 14 publications

References 0 publications

High-pressure polymorphism in L-cysteine: the crystal structures of L-cysteine-III and L-cysteine-IV

High-pressure polymorphism in L-cysteine: the crystal structures of L-cysteine-III and L-cysteine-IV

The solid-state molecular structure of the S-nitroso derivative of l-cysteine ethyl ester hydrochloride

Conformations of Serine in Aqueous Solutions as Revealed by Vibrational Circular Dichroism

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