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Biomedical subjects

M Rico

Publications and source records attributed to M Rico.

116 records · Page 7Linked to original sources
PubMed1984

On the fundamental role of the Glu 2- ... Arg 10+ salt bridge in the folding of isolated ribonuclease A S-peptide.

The fundamental role of the Glu 2- ... Arg 10+ salt bridge in the folding of isolated S-peptide (1-19 N-terminal fragment of Ribonuclease A) is demonstrated from the comparison of the helix contents, at 0 degrees C, of S-peptide and related peptides. Helix contents have been determined from the analysis of proton chemical shift vs. temperature curves. The observed data can be accounted for by assuming that two side-chain interactions contribute to stabilize the 3-13 helix of S-peptide, the salt bridges Glu 2- ... Arg 10+ and Glu 9-... His 12+, the former being more effective. The salt bridge Glu 9- ... Arg 10+ turns to a weaker interaction, a hydrogen bond Glu 2 (C delta = 0) ... Arg 10+, on protonation or esterification of the Glu 2 carboxylate.

Amino Acid Sequence↗
PubMed1983

Low-temperature 1H-NMR evidence of the folding of isolated ribonuclease S-peptide.

The temperature (-7 degrees C to 45 degrees C, pH 5.4) and pH (0 degrees C) dependence of 1H chemical shifts of ribonuclease S-peptide (5 mM, 1 M NaCl) has been measured at 360 MHz. The observed variations evidence the formation of a partial helical structure, involving the fragment Thr-3-Met-13. Two salt-bridges stabilize the helix: those formed by Glu-9- ...His-12+ and Glu-2- ...Arg-10+. The structural features deduced from the 1H-NMR at low temperature for the isolated S-peptide are compatible with the structure shown by the same molecule in the ribonuclease S crystal.

Amino Acid Sequence↗
PubMed1983

1H n.m.r. parameters of the N-terminal 19-residue S-peptide of ribonuclease in aqueous solution.

The 1H n.m.r. chemical shifts and the spin-spin coupling constants of the N-terminal 19-residue S-peptide of ribonuclease A have been measured in a 10 mM solution in D2O, pD 3.0, 27 degrees, at 300 MHz. The titration parameters for end groups Lys-1 and Ala-19 and side chains Lys-1, Glu-2, Lys-7, Glu-9, Arg-10, His-12 and Asp-14 have been determined at 90 MHz. An assignment of observed signals to individual residue protons based upon characteristic shifts, spectral analysis, double resonance, titration shifts and comparison with the spectrum of C-peptide (N-terminal 13-residue) is proposed. Differences in the observed chemical shifts, pKa's and titration shifts with reference to those proposed as "random coil" parameters are not large enough to assume the existence of a significant population of secondary structure in the conditions studied. The H alpha chemical shifts differences can be accounted for by the Phe-8 phenyl ring current for an extended peptide backbone conformation and appropriate values for the torsion angles chi 1 Phe-8 and chi 2 Phe-8.

Amino Acid Sequence↗
PubMed1982

Thermal and 13C-NMR study of the dynamic structure of 1-palmitoyl-2-oleyl-sn-glycero-3-phosphocholine and 1-oleyl-2-palmitoyl-sn-glycero-3-phosphocholine in aqueous dispersions.

Mixed-acid monounsaturated phosphatidylcholines containing palmitate and oleate chains have been synthesized by phospholipase A2 digestion of the appropriate single-acid phosphatidylcholine, followed by reacylation of the lysophosphatidylcholine with the desired fatty acid anhydride. The positional isomers 1-palmitoyl-2-oleyl-sn-glycero-3-phosphocholine and 1-oleyl-2-palmitoyl-sn-phosphocholine have been thus obtained. The thermotropic behavior of these lipids dispersed in excess water has been studied by differential scanning calorimetry. Positional isomers of mixed-acid monounsaturated phosphatidylcholines are found to have different gel to liquid-crystalline transition temperatures and enthalpies. It was found that mixtures of 1-palmitoyl-2-oleyl-sn-glycero-3-phosphocholine with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine or 1,2-distearoyl-sn-glycero-3-phosphocholine exhibited inmiscibility in the phosphatidylcholine gel state. The dynamic structure of 1-palmitoyl-2-oleyl-sn-glycero-3-phosphocholine and 1-oleyl-2-palmitoyl-sn-glycero-3-phosphocholine bilayers has been investigated by measuring the 13C nuclear spin-lattice relaxation times of sonicated aqueous dispersions. No difference was found between the two systems, suggesting that above the thermal transition the presence of the unsaturated acyl group in the 1 or 2 position does not affect significantly the dynamic structure of the bilayer.

Calorimetry, Differential Scanning↗
PubMed1980

Clinical and hemodynamic assessment of the Angell-Shiley porcine xenograft.

Valve replacement with an Angell-Shiley bioprosthesis was accomplished in 449 patients. To evaluate the bioprostheses from this total series, 344 patients who did not undergo associated operation, had no previous operations, or had no other valve substitutes were selected. Hospital mortality was 2.6% for aortic (4 out of 156), 7.2% for mitral (9 out of 125), and 12.7% for multiple-valve replacements (8 out of 63). The 323 patients discharged from the hospital were followed for 6 to 36 months. There were 15 late deaths. Hepatitis, bleeding, thromboembolism, endocarditis, and residual valvular incompetence, always periprosthetic, were the major complications. Forty-five patients with single-valve replacement (16 mitral and 29 aortic) without clinical valve dysfunction were electively recatheterized to assess hemodynamic performance. Measurements were recorded at rest and during exercise on a bicycle ergometer. Functional aortic valve orifice averaged 1.23 +/- 0.33 cm2 and the mean systolic gradient was 21.51 +/- 6.68 mm Hg at rest. During exercise, aortic gradient increased to 26.60 +/- 7.54 mm Hg and mean functional area to 1.51 +/- 0.34 cm2. In the mitral position, the mean diastolic gradient at rest was 8.44 +/- 3.17 mm Hg and the functional orifice area averaged 1.67 +/- 0.51 cm2. Exercise increased the mean gradient to 11.92 +/- 3.8 mm Hg and the mean orifice area to 2.05 +/- 0.57 cm2.

Adolescent↗