Theoretical conformational analysis on elastin analogue tetrapeptide Ac-Ala-Pro-Gly-Gly-NHMe

Summary To investigate the role of the Val residue on stabilizing the γ-helix which is a proposed model conformation of elastin, conformational energy calculations using ECEPP were carried out for Ac-Ala-Pro-Gly-Gly-NHMe which is an analogous tetrapeptide for the sequence Val-Pro-Gly-Gly of elastin....
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Oka, Masahlto [verfasserIn] Baba, Yoshihiro Kagemoto, Aklhiro Nakajima, Akio

Format:	Artikel
Sprache:	Englisch

Erschienen:	1991

Schlagwörter:	Polymer Energy Calculation Conformational Analysis Conformational Energy Conformational Character

Anmerkung:	© Springer-Verlag 1991

Übergeordnetes Werk:	Enthalten in: Polymer bulletin - Springer-Verlag, 1978, 25(1991), 6 vom: Juni, Seite 701-707
Übergeordnetes Werk:	volume:25 ; year:1991 ; number:6 ; month:06 ; pages:701-707

Links:	Volltext

DOI / URN:	10.1007/BF01032668

Katalog-ID:	OLC2042601489

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520			\|a Summary To investigate the role of the Val residue on stabilizing the γ-helix which is a proposed model conformation of elastin, conformational energy calculations using ECEPP were carried out for Ac-Ala-Pro-Gly-Gly-NHMe which is an analogous tetrapeptide for the sequence Val-Pro-Gly-Gly of elastin. The lowest-energy conformation is changed by the amino-acid substitution from Val to Ala residues, however, overall conformational characters in the ensemble of energy-minima of tetrapeptides are fundamentally maintained. The double-bend structure at Pro-Gly-Gly portion of Ac-Ala-Pro-Gly-Gly-NHMe is as favorable as that of Ac-Val-Pro-Gly-Gly-NHMe.
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allfields	10.1007/BF01032668 doi (DE-627)OLC2042601489 (DE-He213)BF01032668-p DE-627 ger DE-627 rakwb eng 540 530 660 VZ BIODIV DE-30 fid Oka, Masahlto verfasserin aut Theoretical conformational analysis on elastin analogue tetrapeptide Ac-Ala-Pro-Gly-Gly-NHMe 1991 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1991 Summary To investigate the role of the Val residue on stabilizing the γ-helix which is a proposed model conformation of elastin, conformational energy calculations using ECEPP were carried out for Ac-Ala-Pro-Gly-Gly-NHMe which is an analogous tetrapeptide for the sequence Val-Pro-Gly-Gly of elastin. The lowest-energy conformation is changed by the amino-acid substitution from Val to Ala residues, however, overall conformational characters in the ensemble of energy-minima of tetrapeptides are fundamentally maintained. The double-bend structure at Pro-Gly-Gly portion of Ac-Ala-Pro-Gly-Gly-NHMe is as favorable as that of Ac-Val-Pro-Gly-Gly-NHMe. Polymer Energy Calculation Conformational Analysis Conformational Energy Conformational Character Baba, Yoshihiro aut Kagemoto, Aklhiro aut Nakajima, Akio aut Enthalten in Polymer bulletin Springer-Verlag, 1978 25(1991), 6 vom: Juni, Seite 701-707 (DE-627)129092916 (DE-600)6871-8 (DE-576)01442861X 0170-0839 nnns volume:25 year:1991 number:6 month:06 pages:701-707 https://doi.org/10.1007/BF01032668 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_22 GBV_ILN_23 GBV_ILN_40 GBV_ILN_65 GBV_ILN_70 GBV_ILN_95 GBV_ILN_2006 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2411 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4315 GBV_ILN_4319 GBV_ILN_4323 AR 25 1991 6 06 701-707
spelling	10.1007/BF01032668 doi (DE-627)OLC2042601489 (DE-He213)BF01032668-p DE-627 ger DE-627 rakwb eng 540 530 660 VZ BIODIV DE-30 fid Oka, Masahlto verfasserin aut Theoretical conformational analysis on elastin analogue tetrapeptide Ac-Ala-Pro-Gly-Gly-NHMe 1991 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1991 Summary To investigate the role of the Val residue on stabilizing the γ-helix which is a proposed model conformation of elastin, conformational energy calculations using ECEPP were carried out for Ac-Ala-Pro-Gly-Gly-NHMe which is an analogous tetrapeptide for the sequence Val-Pro-Gly-Gly of elastin. The lowest-energy conformation is changed by the amino-acid substitution from Val to Ala residues, however, overall conformational characters in the ensemble of energy-minima of tetrapeptides are fundamentally maintained. The double-bend structure at Pro-Gly-Gly portion of Ac-Ala-Pro-Gly-Gly-NHMe is as favorable as that of Ac-Val-Pro-Gly-Gly-NHMe. Polymer Energy Calculation Conformational Analysis Conformational Energy Conformational Character Baba, Yoshihiro aut Kagemoto, Aklhiro aut Nakajima, Akio aut Enthalten in Polymer bulletin Springer-Verlag, 1978 25(1991), 6 vom: Juni, Seite 701-707 (DE-627)129092916 (DE-600)6871-8 (DE-576)01442861X 0170-0839 nnns volume:25 year:1991 number:6 month:06 pages:701-707 https://doi.org/10.1007/BF01032668 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_22 GBV_ILN_23 GBV_ILN_40 GBV_ILN_65 GBV_ILN_70 GBV_ILN_95 GBV_ILN_2006 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2411 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4315 GBV_ILN_4319 GBV_ILN_4323 AR 25 1991 6 06 701-707
allfields_unstemmed	10.1007/BF01032668 doi (DE-627)OLC2042601489 (DE-He213)BF01032668-p DE-627 ger DE-627 rakwb eng 540 530 660 VZ BIODIV DE-30 fid Oka, Masahlto verfasserin aut Theoretical conformational analysis on elastin analogue tetrapeptide Ac-Ala-Pro-Gly-Gly-NHMe 1991 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1991 Summary To investigate the role of the Val residue on stabilizing the γ-helix which is a proposed model conformation of elastin, conformational energy calculations using ECEPP were carried out for Ac-Ala-Pro-Gly-Gly-NHMe which is an analogous tetrapeptide for the sequence Val-Pro-Gly-Gly of elastin. The lowest-energy conformation is changed by the amino-acid substitution from Val to Ala residues, however, overall conformational characters in the ensemble of energy-minima of tetrapeptides are fundamentally maintained. The double-bend structure at Pro-Gly-Gly portion of Ac-Ala-Pro-Gly-Gly-NHMe is as favorable as that of Ac-Val-Pro-Gly-Gly-NHMe. Polymer Energy Calculation Conformational Analysis Conformational Energy Conformational Character Baba, Yoshihiro aut Kagemoto, Aklhiro aut Nakajima, Akio aut Enthalten in Polymer bulletin Springer-Verlag, 1978 25(1991), 6 vom: Juni, Seite 701-707 (DE-627)129092916 (DE-600)6871-8 (DE-576)01442861X 0170-0839 nnns volume:25 year:1991 number:6 month:06 pages:701-707 https://doi.org/10.1007/BF01032668 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_22 GBV_ILN_23 GBV_ILN_40 GBV_ILN_65 GBV_ILN_70 GBV_ILN_95 GBV_ILN_2006 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2411 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4315 GBV_ILN_4319 GBV_ILN_4323 AR 25 1991 6 06 701-707
allfieldsGer	10.1007/BF01032668 doi (DE-627)OLC2042601489 (DE-He213)BF01032668-p DE-627 ger DE-627 rakwb eng 540 530 660 VZ BIODIV DE-30 fid Oka, Masahlto verfasserin aut Theoretical conformational analysis on elastin analogue tetrapeptide Ac-Ala-Pro-Gly-Gly-NHMe 1991 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1991 Summary To investigate the role of the Val residue on stabilizing the γ-helix which is a proposed model conformation of elastin, conformational energy calculations using ECEPP were carried out for Ac-Ala-Pro-Gly-Gly-NHMe which is an analogous tetrapeptide for the sequence Val-Pro-Gly-Gly of elastin. The lowest-energy conformation is changed by the amino-acid substitution from Val to Ala residues, however, overall conformational characters in the ensemble of energy-minima of tetrapeptides are fundamentally maintained. The double-bend structure at Pro-Gly-Gly portion of Ac-Ala-Pro-Gly-Gly-NHMe is as favorable as that of Ac-Val-Pro-Gly-Gly-NHMe. Polymer Energy Calculation Conformational Analysis Conformational Energy Conformational Character Baba, Yoshihiro aut Kagemoto, Aklhiro aut Nakajima, Akio aut Enthalten in Polymer bulletin Springer-Verlag, 1978 25(1991), 6 vom: Juni, Seite 701-707 (DE-627)129092916 (DE-600)6871-8 (DE-576)01442861X 0170-0839 nnns volume:25 year:1991 number:6 month:06 pages:701-707 https://doi.org/10.1007/BF01032668 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_22 GBV_ILN_23 GBV_ILN_40 GBV_ILN_65 GBV_ILN_70 GBV_ILN_95 GBV_ILN_2006 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2411 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4315 GBV_ILN_4319 GBV_ILN_4323 AR 25 1991 6 06 701-707
allfieldsSound	10.1007/BF01032668 doi (DE-627)OLC2042601489 (DE-He213)BF01032668-p DE-627 ger DE-627 rakwb eng 540 530 660 VZ BIODIV DE-30 fid Oka, Masahlto verfasserin aut Theoretical conformational analysis on elastin analogue tetrapeptide Ac-Ala-Pro-Gly-Gly-NHMe 1991 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1991 Summary To investigate the role of the Val residue on stabilizing the γ-helix which is a proposed model conformation of elastin, conformational energy calculations using ECEPP were carried out for Ac-Ala-Pro-Gly-Gly-NHMe which is an analogous tetrapeptide for the sequence Val-Pro-Gly-Gly of elastin. The lowest-energy conformation is changed by the amino-acid substitution from Val to Ala residues, however, overall conformational characters in the ensemble of energy-minima of tetrapeptides are fundamentally maintained. The double-bend structure at Pro-Gly-Gly portion of Ac-Ala-Pro-Gly-Gly-NHMe is as favorable as that of Ac-Val-Pro-Gly-Gly-NHMe. Polymer Energy Calculation Conformational Analysis Conformational Energy Conformational Character Baba, Yoshihiro aut Kagemoto, Aklhiro aut Nakajima, Akio aut Enthalten in Polymer bulletin Springer-Verlag, 1978 25(1991), 6 vom: Juni, Seite 701-707 (DE-627)129092916 (DE-600)6871-8 (DE-576)01442861X 0170-0839 nnns volume:25 year:1991 number:6 month:06 pages:701-707 https://doi.org/10.1007/BF01032668 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_22 GBV_ILN_23 GBV_ILN_40 GBV_ILN_65 GBV_ILN_70 GBV_ILN_95 GBV_ILN_2006 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2411 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4315 GBV_ILN_4319 GBV_ILN_4323 AR 25 1991 6 06 701-707
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author	Oka, Masahlto
spellingShingle	Oka, Masahlto ddc 540 fid BIODIV misc Polymer misc Energy Calculation misc Conformational Analysis misc Conformational Energy misc Conformational Character Theoretical conformational analysis on elastin analogue tetrapeptide Ac-Ala-Pro-Gly-Gly-NHMe
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author_browse	Oka, Masahlto Baba, Yoshihiro Kagemoto, Aklhiro Nakajima, Akio
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title_sort	theoretical conformational analysis on elastin analogue tetrapeptide ac-ala-pro-gly-gly-nhme
title_auth	Theoretical conformational analysis on elastin analogue tetrapeptide Ac-Ala-Pro-Gly-Gly-NHMe
abstract	Summary To investigate the role of the Val residue on stabilizing the γ-helix which is a proposed model conformation of elastin, conformational energy calculations using ECEPP were carried out for Ac-Ala-Pro-Gly-Gly-NHMe which is an analogous tetrapeptide for the sequence Val-Pro-Gly-Gly of elastin. The lowest-energy conformation is changed by the amino-acid substitution from Val to Ala residues, however, overall conformational characters in the ensemble of energy-minima of tetrapeptides are fundamentally maintained. The double-bend structure at Pro-Gly-Gly portion of Ac-Ala-Pro-Gly-Gly-NHMe is as favorable as that of Ac-Val-Pro-Gly-Gly-NHMe. © Springer-Verlag 1991
abstractGer	Summary To investigate the role of the Val residue on stabilizing the γ-helix which is a proposed model conformation of elastin, conformational energy calculations using ECEPP were carried out for Ac-Ala-Pro-Gly-Gly-NHMe which is an analogous tetrapeptide for the sequence Val-Pro-Gly-Gly of elastin. The lowest-energy conformation is changed by the amino-acid substitution from Val to Ala residues, however, overall conformational characters in the ensemble of energy-minima of tetrapeptides are fundamentally maintained. The double-bend structure at Pro-Gly-Gly portion of Ac-Ala-Pro-Gly-Gly-NHMe is as favorable as that of Ac-Val-Pro-Gly-Gly-NHMe. © Springer-Verlag 1991
abstract_unstemmed	Summary To investigate the role of the Val residue on stabilizing the γ-helix which is a proposed model conformation of elastin, conformational energy calculations using ECEPP were carried out for Ac-Ala-Pro-Gly-Gly-NHMe which is an analogous tetrapeptide for the sequence Val-Pro-Gly-Gly of elastin. The lowest-energy conformation is changed by the amino-acid substitution from Val to Ala residues, however, overall conformational characters in the ensemble of energy-minima of tetrapeptides are fundamentally maintained. The double-bend structure at Pro-Gly-Gly portion of Ac-Ala-Pro-Gly-Gly-NHMe is as favorable as that of Ac-Val-Pro-Gly-Gly-NHMe. © Springer-Verlag 1991
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title_short	Theoretical conformational analysis on elastin analogue tetrapeptide Ac-Ala-Pro-Gly-Gly-NHMe
url	https://doi.org/10.1007/BF01032668
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author2	Baba, Yoshihiro Kagemoto, Aklhiro Nakajima, Akio
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up_date	2024-07-03T15:55:28.840Z
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