Helix-coil transitions re-visited
- Autores
- Scheraga, Harold A.; Vila, Jorge Alberto; Ripoll, Daniel R.
- Año de publicación
- 2002
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The thermally-induced helix-coil transition in polyamino acids is a good model for determining the helix-forming propensities of amino acids but not for the two-state folding/unfolding transition in globular proteins. The equilibrium and kinetic treatments of the helix-coil transition are summarized here together with a description of applications to various types of homopolymers and copolymers. Attention is then focused on the helix-coil transition in poly-L-alanine as an example of a non-polar polyamino acid. To render such a non-polar polymer water soluble, it is necessary to introduce polar amino acids such as lysines, but care must be taken as to the location of such polar residues. If they are attached as end groups, as in a triblock copolymer, they do not perturb the helix-forming tendency of the central poly-L-alanine block significantly, but if they are introduced within the sequence of alanine residues, then the hydration properties of the lysines dominate the behavior of the resulting copolymer, thereby leading to erroneous values of the parameters characterizing the helix-forming tendency of the alanines. Neutral but polar residues, such as glutamines, also exhibit hydration-dominating properties but less so than charged lysines. Some details of the calculations for an alanine/glutamine copolymer are presented here. It is concluded that random copolymers based on a neutral water-soluble host provide reliable information about the helix-forming tendencies of amino acid residues that are introduced as guests among such neutral host residues.
Fil: Scheraga, Harold A.. Cornell University; Estados Unidos
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
Fil: Ripoll, Daniel R.. Cornell Theory Center; Estados Unidos - Materia
-
EQUILIBRIUM AND KINETIC TREATMENT
HELIX-FORMING PROPENSITY
HELIX-PROBABILITY PROFILES
POLYAMINO ACIDS
RANDOM COPOLYMERS
ROLE OF HYDRATION - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/118253
Ver los metadatos del registro completo
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Helix-coil transitions re-visitedScheraga, Harold A.Vila, Jorge AlbertoRipoll, Daniel R.EQUILIBRIUM AND KINETIC TREATMENTHELIX-FORMING PROPENSITYHELIX-PROBABILITY PROFILESPOLYAMINO ACIDSRANDOM COPOLYMERSROLE OF HYDRATIONhttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1The thermally-induced helix-coil transition in polyamino acids is a good model for determining the helix-forming propensities of amino acids but not for the two-state folding/unfolding transition in globular proteins. The equilibrium and kinetic treatments of the helix-coil transition are summarized here together with a description of applications to various types of homopolymers and copolymers. Attention is then focused on the helix-coil transition in poly-L-alanine as an example of a non-polar polyamino acid. To render such a non-polar polymer water soluble, it is necessary to introduce polar amino acids such as lysines, but care must be taken as to the location of such polar residues. If they are attached as end groups, as in a triblock copolymer, they do not perturb the helix-forming tendency of the central poly-L-alanine block significantly, but if they are introduced within the sequence of alanine residues, then the hydration properties of the lysines dominate the behavior of the resulting copolymer, thereby leading to erroneous values of the parameters characterizing the helix-forming tendency of the alanines. Neutral but polar residues, such as glutamines, also exhibit hydration-dominating properties but less so than charged lysines. Some details of the calculations for an alanine/glutamine copolymer are presented here. It is concluded that random copolymers based on a neutral water-soluble host provide reliable information about the helix-forming tendencies of amino acid residues that are introduced as guests among such neutral host residues.Fil: Scheraga, Harold A.. Cornell University; Estados UnidosFil: 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"; ArgentinaFil: Ripoll, Daniel R.. Cornell Theory Center; Estados UnidosElsevier Science2002-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/118253Scheraga, Harold A.; Vila, Jorge Alberto; Ripoll, Daniel R.; Helix-coil transitions re-visited; Elsevier Science; Biophysical Chemistry; 101-102; 12-2002; 255-2650301-4622CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/S0301-4622(02)00175-8info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0301462202001758?via%3Dihubinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:38:15Zoai:ri.conicet.gov.ar:11336/118253instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:38:15.674CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Helix-coil transitions re-visited |
title |
Helix-coil transitions re-visited |
spellingShingle |
Helix-coil transitions re-visited Scheraga, Harold A. EQUILIBRIUM AND KINETIC TREATMENT HELIX-FORMING PROPENSITY HELIX-PROBABILITY PROFILES POLYAMINO ACIDS RANDOM COPOLYMERS ROLE OF HYDRATION |
title_short |
Helix-coil transitions re-visited |
title_full |
Helix-coil transitions re-visited |
title_fullStr |
Helix-coil transitions re-visited |
title_full_unstemmed |
Helix-coil transitions re-visited |
title_sort |
Helix-coil transitions re-visited |
dc.creator.none.fl_str_mv |
Scheraga, Harold A. Vila, Jorge Alberto Ripoll, Daniel R. |
author |
Scheraga, Harold A. |
author_facet |
Scheraga, Harold A. Vila, Jorge Alberto Ripoll, Daniel R. |
author_role |
author |
author2 |
Vila, Jorge Alberto Ripoll, Daniel R. |
author2_role |
author author |
dc.subject.none.fl_str_mv |
EQUILIBRIUM AND KINETIC TREATMENT HELIX-FORMING PROPENSITY HELIX-PROBABILITY PROFILES POLYAMINO ACIDS RANDOM COPOLYMERS ROLE OF HYDRATION |
topic |
EQUILIBRIUM AND KINETIC TREATMENT HELIX-FORMING PROPENSITY HELIX-PROBABILITY PROFILES POLYAMINO ACIDS RANDOM COPOLYMERS ROLE OF HYDRATION |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.3 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The thermally-induced helix-coil transition in polyamino acids is a good model for determining the helix-forming propensities of amino acids but not for the two-state folding/unfolding transition in globular proteins. The equilibrium and kinetic treatments of the helix-coil transition are summarized here together with a description of applications to various types of homopolymers and copolymers. Attention is then focused on the helix-coil transition in poly-L-alanine as an example of a non-polar polyamino acid. To render such a non-polar polymer water soluble, it is necessary to introduce polar amino acids such as lysines, but care must be taken as to the location of such polar residues. If they are attached as end groups, as in a triblock copolymer, they do not perturb the helix-forming tendency of the central poly-L-alanine block significantly, but if they are introduced within the sequence of alanine residues, then the hydration properties of the lysines dominate the behavior of the resulting copolymer, thereby leading to erroneous values of the parameters characterizing the helix-forming tendency of the alanines. Neutral but polar residues, such as glutamines, also exhibit hydration-dominating properties but less so than charged lysines. Some details of the calculations for an alanine/glutamine copolymer are presented here. It is concluded that random copolymers based on a neutral water-soluble host provide reliable information about the helix-forming tendencies of amino acid residues that are introduced as guests among such neutral host residues. Fil: Scheraga, Harold A.. Cornell University; Estados Unidos 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 Fil: Ripoll, Daniel R.. Cornell Theory Center; Estados Unidos |
description |
The thermally-induced helix-coil transition in polyamino acids is a good model for determining the helix-forming propensities of amino acids but not for the two-state folding/unfolding transition in globular proteins. The equilibrium and kinetic treatments of the helix-coil transition are summarized here together with a description of applications to various types of homopolymers and copolymers. Attention is then focused on the helix-coil transition in poly-L-alanine as an example of a non-polar polyamino acid. To render such a non-polar polymer water soluble, it is necessary to introduce polar amino acids such as lysines, but care must be taken as to the location of such polar residues. If they are attached as end groups, as in a triblock copolymer, they do not perturb the helix-forming tendency of the central poly-L-alanine block significantly, but if they are introduced within the sequence of alanine residues, then the hydration properties of the lysines dominate the behavior of the resulting copolymer, thereby leading to erroneous values of the parameters characterizing the helix-forming tendency of the alanines. Neutral but polar residues, such as glutamines, also exhibit hydration-dominating properties but less so than charged lysines. Some details of the calculations for an alanine/glutamine copolymer are presented here. It is concluded that random copolymers based on a neutral water-soluble host provide reliable information about the helix-forming tendencies of amino acid residues that are introduced as guests among such neutral host residues. |
publishDate |
2002 |
dc.date.none.fl_str_mv |
2002-12 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/118253 Scheraga, Harold A.; Vila, Jorge Alberto; Ripoll, Daniel R.; Helix-coil transitions re-visited; Elsevier Science; Biophysical Chemistry; 101-102; 12-2002; 255-265 0301-4622 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/118253 |
identifier_str_mv |
Scheraga, Harold A.; Vila, Jorge Alberto; Ripoll, Daniel R.; Helix-coil transitions re-visited; Elsevier Science; Biophysical Chemistry; 101-102; 12-2002; 255-265 0301-4622 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/S0301-4622(02)00175-8 info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0301462202001758?via%3Dihub |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier Science |
publisher.none.fl_str_mv |
Elsevier Science |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1844613208327847936 |
score |
13.070432 |