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- Publications
- Influence
Conformation and aggregation of melittin: dependence on pH and concentration.
- J. Bello, H. R. Bello, E. Granados
- Chemistry, Medicine
- Biochemistry
- 2 February 1982
Melittin, a 26-residue peptide from bee venom, is transformed from a largely random to a largely alpha-helical conformation at elevated pH. At 3 x 10(-5) M melittin, circular dichroism spectra show a… Expand
Ultraviolet absorbance changes accompanying the denaturation of soluble collagen and antelocollagen.
Interaction of sodium dodecyl sulfate with tyrosyl chromophores in ribonuclease A and model compounds.
- E. P. Pittz, J. Bello
- Chemistry, Medicine
- Archives of biochemistry and biophysics
- 1 November 1971
Abstract Ultraviolet difference spectra, solvent perturbation difference spectra, and temperature perturbation difference spectra indicate that tyrosyl residues of model compounds are affected by… Expand
Studies on bovine pancreatic ribonuclease A and model compounds in aqueous 2-methyl-2,4-pentanediol. I. Amino acid solubility, thermal reversibility of ribonuclease A, and preferential hydration of…
- E. P. Pittz, J. Bello
- Chemistry, Medicine
- Archives of biochemistry and biophysics
- 1 October 1971
Abstract For X-ray investigations, RNase-A is crystallized from a mixture of 55% 2-methyl-2,4-pentanediol (MPD) and 45% water. Interactions of RNase-A and amino acids with this solvent have been… Expand
The mechanism of gelation of gelatin. The influence of pH, concentration, time and dilute electrolyte on the gelation of gelatin and modified gelatins.
- J. Bello, H. R. Bello, J. Vinograd
- Chemistry, Medicine
- Biochimica et biophysica acta
- 1962
Abstract The effects of concentration, pH, time and dilute electrolyte on the melting points of gels of gelatin and chemically modified gelatins have been investigated. At 1–5% concentration the… Expand
Conformational studies of anionic melittin analogues: Effect of peptide concentration, pH, ionic strength, and temperature—models for protein folding and halophilic proteins
- K. Ramalingam, S. Aimoto, J. Bello
- Chemistry, Medicine
- Biopolymers
- 1 August 1992
Melittin (MLT), a 26‐residue cationic (net charge +5 at pH 7.2) peptide from bee venom, is well known to be a monomeric, approximately random coil; but when its charges are reduced by titration, by… Expand
Conformational changes in melittin upon complexation with an anionic melittin analog
- K. Ramalingam, J. Bello, S. Aimoto
- Chemistry, Medicine
- FEBS letters
- 16 December 1991
Melittin and its Glu‐(7,21,22,23,24) analog upon mixing in equimolar concentrations form a hybrid oligomer with significant helical structure, in conditions in which each peptide separately adopts a… Expand
Tertiary Structure of Ribonuclease
A model is proposed of the polypeptide chain in bovine pancreatic ribonuclease based on a 2 Å electron density map involving 7,294 reflexions and data from seven heavy atom derivatives. The molecule… Expand
Poly ICL-CM dextran: an interferon inducer of reduced toxicity.
- E. Granados, J. Dawidzik, J. O'Malley, M. McGarry, J. Bello
- Chemistry, Medicine
- Journal of interferon research
- 1984
We have prepared soluble complexes of poly ICL-CM dextran that are as effective interferon IFN inducers, in mice and in rhesus monkeys, as poly ICLC. Toxicity testing was carried out in mice and,… Expand