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Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms.
- V. Muñoz, L. Serrano
- Chemistry, Medicine
- Biopolymers
- 15 April 1997
In this work we present the development of the multiple sequence approximation (AGADIRms) and the standard one-sequence approximation (AGADIRls) within the framework of AGADIR's alpha-helix formation… Expand
Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides.
- V. Muñoz, L. Serrano
- Chemistry, Medicine
- Journal of molecular biology
- 20 January 1995
Explaining the helical behaviour of amino acid sequences in solution could be one of the first steps in solving the protein folding problem in a rational way. The information about the conformational… Expand
Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence.
- V. Muñoz, L. Serrano
- Chemistry, Medicine
- Journal of molecular biology
- 20 January 1995
Explaining the helical behaviour of amino acid sequences without tertiary interactions, in aqueous solution, could be considered one of the first steps to solve the protein folding problem in a… Expand
Alpha-helix structure in Alzheimer's disease aggregates of tau-protein.
- M. Sadqi, F. Hernández, +4 authors V. Muñoz
- Chemistry, Medicine
- Biochemistry
- 7 May 2002
The discovery of beta-sheet structure in Alzheimer's amyloid fibrils, and then in many other disease-related protein fibrils, has led to the widely believed view that beta-sheet formation is the… Expand
Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales.
- V. Muñoz, L. Serrano
- Medicine
- Proteins
- 1994
Today there are several different experimental scales for the intrinsic alpha-helix as well as beta-strand propensities of the 20 amino acids obtained from the thermodynamic analysis of various model… Expand
[Environmental contamination with Toxocara sp. eggs in public squares and parks from Santiago, Chile, 1999].
- D. Castillo, C. Paredes, +4 authors H. Schenone
- Biology, Medicine
- Boletin chileno de parasitologia
- 1 July 2000
Most of cases of visceral larva migrans syndrome are caused by Toxocara canis larvae. Man acquires the infection by accidental ingestion of ripe eggs of the helminth. In order to find out the… Expand
Kinetic characterization of the chemotactic protein from Escherichia coli, CheY. Kinetic analysis of the inverse hydrophobic effect.
- V. Muñoz, E. López, M. Jager, L. Serrano
- Chemistry, Medicine
- Biochemistry
- 17 May 1994
CheY, the 129 amino acid chemotactic protein from Escherichia coli, is a good model for studying the folding process of the parallel alpha/beta family of proteins. A study of the folding kinetics of… Expand
Local versus nonlocal interactions in protein folding and stability--an experimentalist's point of view.
- V. Muñoz, L. Serrano
- Computer Science, Medicine
- Folding & design
- 1 August 1996
TLDR
Position dependence of non-polar amino acid intrinsic helical propensities.
- M. Petukhov, V. Muñoz, N. Yumoto, S. Yoshikawa, L. Serrano
- Chemistry, Medicine
- Journal of molecular biology
- 24 April 1998
Until now and based on the success of the helix/coil transition theory it has been assumed that the alpha-helical propensities of the amino acids are position independent. This has been critical to… Expand
Interplay between hydrophobic cluster and loop propensity in beta-hairpin formation.
- J. F. Espinosa, V. Muñoz, S. Gellman
- Chemistry, Medicine
- Journal of molecular biology
- 23 February 2001
Autonomously folding beta-hairpins have recently emerged as powerful tools for elucidating the origins of antiparallel beta-sheet folding preferences. Analysis of such model systems has suggested… Expand