Heme Distortions in Sperm-Whale Carbonmonoxy Myoglobin: Correlations between Rotational Strengths and Heme Distortions in MD-Generated Structures
The authors have investigated the effects of heme rotational isomerism in sperm-whale carbonmonoxy myoglobin using computational techniques. Several molecular dynamics simulations have been performed for the two rotational isomers A and B, which are related by a 180{degree} rotation around the {alph...
Main Authors: | , , , , , |
---|---|
Language: | unknown |
Published: |
2009
|
Subjects: | |
Online Access: | http://www.osti.gov/servlets/purl/759889 https://www.osti.gov/biblio/759889 |
id |
ftosti:oai:osti.gov:759889 |
---|---|
record_format |
openpolar |
spelling |
ftosti:oai:osti.gov:759889 2023-07-30T04:07:06+02:00 Heme Distortions in Sperm-Whale Carbonmonoxy Myoglobin: Correlations between Rotational Strengths and Heme Distortions in MD-Generated Structures KIEFL,CHRISTOPH SCREERAMA,NARASIMHA LU,YI QIU,YAN SHELNUTT,JOHN A. WOODY,ROBERT W. 2009-12-16 application/pdf http://www.osti.gov/servlets/purl/759889 https://www.osti.gov/biblio/759889 unknown http://www.osti.gov/servlets/purl/759889 https://www.osti.gov/biblio/759889 59 BASIC BIOLOGICAL SCIENCES HEME ISOMERS MYOGLOBIN PROTEINS ROTATION MOLECULAR DYNAMICS METHOD CETACEANS PROTEIN STRUCTURE DEFORMATION 2009 ftosti 2023-07-11T08:36:43Z The authors have investigated the effects of heme rotational isomerism in sperm-whale carbonmonoxy myoglobin using computational techniques. Several molecular dynamics simulations have been performed for the two rotational isomers A and B, which are related by a 180{degree} rotation around the {alpha}-{gamma} axis of the heme, of sperm-whale carbonmonoxy myoglobin in water. Both neutron diffraction and NMR structures were used as starting structures. In the absence of an experimental structure, the structure of isomer B was generated by rotating the heme in the structure of isomer A. Distortions of the heme from planarity were characterized by normal coordinate structural decomposition and by the angle of twist of the pyrrole rings from the heme plane. The heme distortions of the neutron diffraction structure were conserved in the MD trajectories, but in the NMR-based trajectories, where the heme distortions are less well defined, they differ from the original heme deformations. The protein matrix induced similar distortions on the heroes in orientations A and B. The results suggest that the binding site prefers a particular macrocycle conformation, and a 180{degree} rotation of the heme does not significantly alter the protein's preference for this conformation. The intrinsic rotational strengths of the two Soret transitions, separated according to their polarization in the heme plane, show strong correlations with the ruf-deformation and the average twist angle of the pyrrole rings. The total rotational strength, which includes contributions from the chromophores in the protein, shows a weaker correlation with heme distortions. Other/Unknown Material Sperm whale SciTec Connect (Office of Scientific and Technical Information - OSTI, U.S. Department of Energy) |
institution |
Open Polar |
collection |
SciTec Connect (Office of Scientific and Technical Information - OSTI, U.S. Department of Energy) |
op_collection_id |
ftosti |
language |
unknown |
topic |
59 BASIC BIOLOGICAL SCIENCES HEME ISOMERS MYOGLOBIN PROTEINS ROTATION MOLECULAR DYNAMICS METHOD CETACEANS PROTEIN STRUCTURE DEFORMATION |
spellingShingle |
59 BASIC BIOLOGICAL SCIENCES HEME ISOMERS MYOGLOBIN PROTEINS ROTATION MOLECULAR DYNAMICS METHOD CETACEANS PROTEIN STRUCTURE DEFORMATION KIEFL,CHRISTOPH SCREERAMA,NARASIMHA LU,YI QIU,YAN SHELNUTT,JOHN A. WOODY,ROBERT W. Heme Distortions in Sperm-Whale Carbonmonoxy Myoglobin: Correlations between Rotational Strengths and Heme Distortions in MD-Generated Structures |
topic_facet |
59 BASIC BIOLOGICAL SCIENCES HEME ISOMERS MYOGLOBIN PROTEINS ROTATION MOLECULAR DYNAMICS METHOD CETACEANS PROTEIN STRUCTURE DEFORMATION |
description |
The authors have investigated the effects of heme rotational isomerism in sperm-whale carbonmonoxy myoglobin using computational techniques. Several molecular dynamics simulations have been performed for the two rotational isomers A and B, which are related by a 180{degree} rotation around the {alpha}-{gamma} axis of the heme, of sperm-whale carbonmonoxy myoglobin in water. Both neutron diffraction and NMR structures were used as starting structures. In the absence of an experimental structure, the structure of isomer B was generated by rotating the heme in the structure of isomer A. Distortions of the heme from planarity were characterized by normal coordinate structural decomposition and by the angle of twist of the pyrrole rings from the heme plane. The heme distortions of the neutron diffraction structure were conserved in the MD trajectories, but in the NMR-based trajectories, where the heme distortions are less well defined, they differ from the original heme deformations. The protein matrix induced similar distortions on the heroes in orientations A and B. The results suggest that the binding site prefers a particular macrocycle conformation, and a 180{degree} rotation of the heme does not significantly alter the protein's preference for this conformation. The intrinsic rotational strengths of the two Soret transitions, separated according to their polarization in the heme plane, show strong correlations with the ruf-deformation and the average twist angle of the pyrrole rings. The total rotational strength, which includes contributions from the chromophores in the protein, shows a weaker correlation with heme distortions. |
author |
KIEFL,CHRISTOPH SCREERAMA,NARASIMHA LU,YI QIU,YAN SHELNUTT,JOHN A. WOODY,ROBERT W. |
author_facet |
KIEFL,CHRISTOPH SCREERAMA,NARASIMHA LU,YI QIU,YAN SHELNUTT,JOHN A. WOODY,ROBERT W. |
author_sort |
KIEFL,CHRISTOPH |
title |
Heme Distortions in Sperm-Whale Carbonmonoxy Myoglobin: Correlations between Rotational Strengths and Heme Distortions in MD-Generated Structures |
title_short |
Heme Distortions in Sperm-Whale Carbonmonoxy Myoglobin: Correlations between Rotational Strengths and Heme Distortions in MD-Generated Structures |
title_full |
Heme Distortions in Sperm-Whale Carbonmonoxy Myoglobin: Correlations between Rotational Strengths and Heme Distortions in MD-Generated Structures |
title_fullStr |
Heme Distortions in Sperm-Whale Carbonmonoxy Myoglobin: Correlations between Rotational Strengths and Heme Distortions in MD-Generated Structures |
title_full_unstemmed |
Heme Distortions in Sperm-Whale Carbonmonoxy Myoglobin: Correlations between Rotational Strengths and Heme Distortions in MD-Generated Structures |
title_sort |
heme distortions in sperm-whale carbonmonoxy myoglobin: correlations between rotational strengths and heme distortions in md-generated structures |
publishDate |
2009 |
url |
http://www.osti.gov/servlets/purl/759889 https://www.osti.gov/biblio/759889 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
http://www.osti.gov/servlets/purl/759889 https://www.osti.gov/biblio/759889 |
_version_ |
1772820203147624448 |