Nmr analyses of conformations of linear peptides in solution

Miyazawa, Tatsuo; Higashijima, Tsutomu

doi:10.1002/bip.1981.360200917

Cited by 8 publications

(2 citation statements)

References 21 publications

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“…The Q(5) AB/AT constant, however, is small and positive. Since the CaHa proton chemical shifts varied linearly with temperature, no apparent change in structure (on the NMR time scale) occurred over the temperature range examined here (21). The data thus imply that the Q(5) amide proton is involved in an intramolecular hydrogen bond (22,23).…”

Section: Nmr Heptapeptide Chemical Shift and Temperature Dependence Amentioning

confidence: 64%

Nuclear magnetic resonance spectroscopic and computer-stimulated structural analyses of a heptapeptide sequence found around the N-glycosylation site of a proline-rich glycoprotein from human parotid saliva

Loomis¹,

Bhandary²,

Tseng³

et al. 1987

Biophysical Journal

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The proline-rich glycoprotein from human parotid saliva has a common heptapeptide sequence around four of six N-glycosylation sites (Maeda, N., H. S. Kim, E. A. Azen, and O. J. Smithies, 1985, J. Biol. Chem., 20:11123-11130). A synthetic model of the heptamer protein sequence, NH2-Q(1)-G(2)-G(3)-N(4)-Q(5)-S(6)-Q(7)-CONH2, was examined by nuclear magnetic resonance (NMR) spectroscopy and the ECEPP/2-VAO4A (Empirical Conformation Energy Program for Peptides) energy minimization computer algorithm (Scheraga, H. A., 1982, Quantum Chemistry Program Exchange, 454; Powell, M. J. D., 1964, Quantum Chemistry Program Exchange, 60). The NMR spectrum was almost completely assigned in dimethylsulfoxide-d6 (DMSO), and the amide chemical shift temperature dependence, phi dihedral angles, and chi 1 rotamer populations elucidated. These data indicated that a significant population of the heptamer could exist as a type I beta-turn [4----1 between Q(5) and G(2)] and/or a type II' beta-turn [4----1 between (Q)5 and G(2) and/or a gamma-turn [3----1 between Q(5) and G(3)] with the amino acid chi 1 torsion angles weighted toward the gauche- conformation. Starting from these three possible conformations, the ECEPP/2-VAO4A rigid geometry energy minimization program was used to find the localized predominant in vacuo structures of this heptapeptide sequence. The type II' beta-turn conformation best fits the data based on internuclear hydrogen-bonding distances, minimum potential energy considerations, and the NMR parameters.

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Section: Nmr Heptapeptide Chemical Shift and Temperature Dependence Amentioning

confidence: 64%

Nuclear magnetic resonance spectroscopic and computer-stimulated structural analyses of a heptapeptide sequence found around the N-glycosylation site of a proline-rich glycoprotein from human parotid saliva

Loomis¹,

Bhandary²,

Tseng³

et al. 1987

Biophysical Journal

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“…Variations greater than experimental error were found for Glu 2, Ala 4, Ala 5 and His 12, 3 J~~c~ values of which decreased with temperature. JHNCH NH resonances of S-peptide the literature as indicators of secondary structure (15,16).…”

Section: Temperature Dependence Of Linewidths Andmentioning

confidence: 99%

NH resonances of Ribonuclease S‐peptide in aqueous solution. Low temperature n.m.r. study

Nieto

Rico

Santoro

et al. 1985

International Journal of Peptide and Protein Research

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A detailed study of the NH resonances of Ribonuclease‐S‐peptide (1–19 N‐terminal fragment of Ribonuclease A) has been carried out in H2O, pH 3.0, in the temperature range 1–31, and ionic strength 0–1 M. Individual assignments of all NH amide signals have been achieved by means of extensive double resonance experiments. The folding of S‐peptide at low temperature has been monitored by examination of the several NH resonance parameters: first, the non‐linearity of chemical shift vs. temperature plots; second, the selective broadening observed for signals assigned to residues 3–13; and third, the decrease of 3JHNCH coupling constants belonging to this region of the polypeptide chain. All these results are in agreement with the formation of a folded structure at low temperature, which is similar to the one found for the S‐peptide in the RNase S crystal.

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Vibrational spectroscopic analysis of LD‐sequential, bacterial cell wall peptides: An IR and raman study

Naumann

Labischinski

Rönspeck³

et al. 1987

Biopolymers

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SynopsisThe synthetic, zwitterionic bacterial cell wall peptides-D-GluY-L-Lys, D-GhY-L-Lys-D-da, D-G1uY-L-Lys-D-Ala-D-Ala, and L-Ala-D-G1uY-L-Lys-D-Ala-D-Ala-have been investigated in the crystalline and aqueous solution state applying ir and Raman spectroscopy. Additionally, aqueous solutions of the tetra-and pentapeptide have been investigated by CD spectroscopic techniques. Apart from the dipeptide, whose spectral features were dominated by end-group vibrations, the corresponding ir and Raman active bands of the crystalline peptides in the amide and skeletal regions were found at similar wave numbers, thus suggesting an analogous three-dimensional structure of these compounds. Dominant amide A, I, 11, and I11 bands near 3275, 1630, 1540, and 1220-1250 cm-', respectively, in the ir are interpreted in favor of an intermolecularly hydrogenbonded, P-like structure. The absence of any amide components near 1680-1690 cm-', together with the presence of strong amide bands near 1630 cm-', and weak bands near 1660 cm-' in the ir, which, conversely, were found in the Raman spectra as weak and strong bands, but at corresponding wave numbers, is taken as strong evidence for the presence of the unusual, parallel-arranged p-structure. On the basis of comparative theoretical considerations, a parallelarranged, "P-type ring" conformation [P. De Santis, S. Morosetti, and R. Rizzo (1974) Macromolecules 7 , 52-58] is hypothesized. The solubilized peptides exhibited distinct similarities with their crystalline counterparts in respect to frequency values and relative intensities of the corresponding ir and Raman-active amide I/I' components, and of some Raman bands in the skeletal region. This is interpreted in terms of residual short-range order, persisting even in aqueous solution. We concluded that the peptides show a strong propensity to form hydrated, strongly associated aggregates in water. On the basis of amide I/I' band positions, stable, intramolecular interactions via the amide groups are discarded for the solubilized peptides. Complementarily, the CD data obtained suggest the presence of weakly bent, "open-turn"-like structures for the tetra-and pentapeptide in aqueous solution.

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Nmr analyses of conformations of linear peptides in solution

Cited by 8 publications

References 21 publications

Nuclear magnetic resonance spectroscopic and computer-stimulated structural analyses of a heptapeptide sequence found around the N-glycosylation site of a proline-rich glycoprotein from human parotid saliva

Nuclear magnetic resonance spectroscopic and computer-stimulated structural analyses of a heptapeptide sequence found around the N-glycosylation site of a proline-rich glycoprotein from human parotid saliva

NH resonances of Ribonuclease S‐peptide in aqueous solution. Low temperature n.m.r. study

Vibrational spectroscopic analysis of LD‐sequential, bacterial cell wall peptides: An IR and raman study

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