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dc.contributor.author
Vila, Jorge Alberto
dc.contributor.author
Ripoll, Raniel R.
dc.contributor.author
Baldoni, Hector Armando
dc.contributor.author
Scheraga, Harold A.
dc.date.available
2020-11-18T18:59:52Z
dc.date.issued
2002-03
dc.identifier.citation
Vila, Jorge Alberto; Ripoll, Raniel R.; Baldoni, Hector Armando; Scheraga, Harold A.; Unblocked statistical-coil tetrapeptides and pentapeptides in aqueous solution: a theoretical study; Springer; Journal Of Biomolecular Nmr; 24; 3; 3-2002; 245-262
dc.identifier.issn
0925-2738
dc.identifier.uri
http://hdl.handle.net/11336/118627
dc.description.abstract
NMR studies of the molecular conformations of peptides and proteins rely on a comparison of the relevant spectral parameters with the corresponding values for so-called statistical-coilpolypeptides. For this reason, it is necessary to characterize the experimental ensemble of states populated by statistical-coilpeptides. Such a characterization, however, has proven to be both difficult and sensitive to changes in many environmental parameters such as solvent composition, temperature, pH, as well as the neighboring amino acids in the sequence. As a consequence, a series of significant discrepancies has been reported for some experimentally observed parameters, such as chemical shifts, or vicinal coupling constants, 3JNHα, whose values appear to be incompatible with a statistical-coilensemble. In this work, we report the results of a molecular mechanics study of a series of unblocked tetra- and pentapeptides under different pH conditions. These calculations were carried out with explicit consideration of both the coupling between the process of proton binding/release and conformation adopted by the molecule at a given pH and the contribution of the conformational entropy to the total free energy. Good agreement was found between the calculated and experimentally determined values of the vicinal coupling constant, 3JNHα, the α-proton chemical shift, and the 13Cαchemical shift. All the evidence accumulated in these theoretical calculations helps to rationalize some of the unsettled anomalies observed experimentally, and to provide an understanding of the effect of pH and amino acid sequence on the conformational preferences of statistical-coilpeptides.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
CHEMICAL SHIFTS
dc.subject
CONFORMATIONAL SEARCH
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RANDOM COILS
dc.subject
SOLVATION FREE ENERGY
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STATISTICAL COILS
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VICINAL COUPLING CONSTANT
dc.subject.classification
Física Atómica, Molecular y Química
dc.subject.classification
Ciencias Físicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Unblocked statistical-coil tetrapeptides and pentapeptides in aqueous solution: a theoretical study
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-09-03T19:25:38Z
dc.journal.volume
24
dc.journal.number
3
dc.journal.pagination
245-262
dc.journal.pais
Alemania
dc.journal.ciudad
Berlin
dc.description.fil
Fil: Vila, Jorge Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi". Universidad Nacional de San Luis. Facultad de Ciencias Físico, Matemáticas y Naturales. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi"; Argentina
dc.description.fil
Fil: Ripoll, Raniel R.. Cornell University; Estados Unidos
dc.description.fil
Fil: Baldoni, Hector Armando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi". Universidad Nacional de San Luis. Facultad de Ciencias Físico, Matemáticas y Naturales. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi"; Argentina
dc.description.fil
Fil: Scheraga, Harold A.. Cornell University; Estados Unidos
dc.journal.title
Journal Of Biomolecular Nmr
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1023/A:1021633403715
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1023%2FA%3A1021633403715
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