The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.

The flexibility in the structure of calmodulin (CaM) allows its binding to over 300 target proteins in the cell. To investigate the structure-function relationship of CaM, we combined methods of computer simulation and experiments based on circular dichroism (CD) to investigate the structural charac...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Qian Wang, Kao-Chen Liang, Arkadiusz Czader, M Neal Waxham, Margaret S Cheung
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/6edcb134dcbb4612b37be7704b0fa8fe
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:6edcb134dcbb4612b37be7704b0fa8fe
record_format	dspace
spelling	oai:doaj.org-article:6edcb134dcbb4612b37be7704b0fa8fe2021-11-18T05:50:23ZThe effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.1553-734X1553-735810.1371/journal.pcbi.1002114https://doaj.org/article/6edcb134dcbb4612b37be7704b0fa8fe2011-07-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21829336/?tool=EBIhttps://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358The flexibility in the structure of calmodulin (CaM) allows its binding to over 300 target proteins in the cell. To investigate the structure-function relationship of CaM, we combined methods of computer simulation and experiments based on circular dichroism (CD) to investigate the structural characteristics of CaM that influence its target recognition in crowded cell-like conditions. We developed a unique multiscale solution of charges computed from quantum chemistry, together with protein reconstruction, coarse-grained molecular simulations, and statistical physics, to represent the charge distribution in the transition from apoCaM to holoCaM upon calcium binding. Computationally, we found that increased levels of macromolecular crowding, in addition to calcium binding and ionic strength typical of that found inside cells, can impact the conformation, helicity and the EF hand orientation of CaM. Because EF hand orientation impacts the affinity of calcium binding and the specificity of CaM's target selection, our results may provide unique insight into understanding the promiscuous behavior of calmodulin in target selection inside cells.Qian WangKao-Chen LiangArkadiusz CzaderM Neal WaxhamMargaret S CheungPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 7, Iss 7, p e1002114 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Qian Wang Kao-Chen Liang Arkadiusz Czader M Neal Waxham Margaret S Cheung The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.
description	The flexibility in the structure of calmodulin (CaM) allows its binding to over 300 target proteins in the cell. To investigate the structure-function relationship of CaM, we combined methods of computer simulation and experiments based on circular dichroism (CD) to investigate the structural characteristics of CaM that influence its target recognition in crowded cell-like conditions. We developed a unique multiscale solution of charges computed from quantum chemistry, together with protein reconstruction, coarse-grained molecular simulations, and statistical physics, to represent the charge distribution in the transition from apoCaM to holoCaM upon calcium binding. Computationally, we found that increased levels of macromolecular crowding, in addition to calcium binding and ionic strength typical of that found inside cells, can impact the conformation, helicity and the EF hand orientation of CaM. Because EF hand orientation impacts the affinity of calcium binding and the specificity of CaM's target selection, our results may provide unique insight into understanding the promiscuous behavior of calmodulin in target selection inside cells.
format	article
author	Qian Wang Kao-Chen Liang Arkadiusz Czader M Neal Waxham Margaret S Cheung
author_facet	Qian Wang Kao-Chen Liang Arkadiusz Czader M Neal Waxham Margaret S Cheung
author_sort	Qian Wang
title	The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.
title_short	The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.
title_full	The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.
title_fullStr	The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.
title_full_unstemmed	The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.
title_sort	effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/6edcb134dcbb4612b37be7704b0fa8fe
work_keys_str_mv	AT qianwang theeffectofmacromolecularcrowdingionicstrengthandcalciumbindingoncalmodulindynamics AT kaochenliang theeffectofmacromolecularcrowdingionicstrengthandcalciumbindingoncalmodulindynamics AT arkadiuszczader theeffectofmacromolecularcrowdingionicstrengthandcalciumbindingoncalmodulindynamics AT mnealwaxham theeffectofmacromolecularcrowdingionicstrengthandcalciumbindingoncalmodulindynamics AT margaretscheung theeffectofmacromolecularcrowdingionicstrengthandcalciumbindingoncalmodulindynamics AT qianwang effectofmacromolecularcrowdingionicstrengthandcalciumbindingoncalmodulindynamics AT kaochenliang effectofmacromolecularcrowdingionicstrengthandcalciumbindingoncalmodulindynamics AT arkadiuszczader effectofmacromolecularcrowdingionicstrengthandcalciumbindingoncalmodulindynamics AT mnealwaxham effectofmacromolecularcrowdingionicstrengthandcalciumbindingoncalmodulindynamics AT margaretscheung effectofmacromolecularcrowdingionicstrengthandcalciumbindingoncalmodulindynamics
_version_	1718424792469602304

The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.

Ejemplares similares