Modelling multi-protein complexes using PELDOR distance measurements for rigid body minimisation experiments using XPLOR-NIH

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Modelling multi-protein complexes using PELDOR distance measurements for rigid body minimisation experiments using XPLOR-NIH. / Hammond, Colin M; Owen-Hughes, Tom; Norman, David G.

In: Methods, Vol. 70, No. 2-3, 12.2014, p. 139-53.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hammond, CM, Owen-Hughes, T & Norman, DG 2014, 'Modelling multi-protein complexes using PELDOR distance measurements for rigid body minimisation experiments using XPLOR-NIH', Methods, vol. 70, no. 2-3, pp. 139-53. https://doi.org/10.1016/j.ymeth.2014.10.028

APA

Hammond, C. M., Owen-Hughes, T., & Norman, D. G. (2014). Modelling multi-protein complexes using PELDOR distance measurements for rigid body minimisation experiments using XPLOR-NIH. Methods, 70(2-3), 139-53. https://doi.org/10.1016/j.ymeth.2014.10.028

Vancouver

Hammond CM, Owen-Hughes T, Norman DG. Modelling multi-protein complexes using PELDOR distance measurements for rigid body minimisation experiments using XPLOR-NIH. Methods. 2014 Dec;70(2-3):139-53. https://doi.org/10.1016/j.ymeth.2014.10.028

Author

Hammond, Colin M ; Owen-Hughes, Tom ; Norman, David G. / Modelling multi-protein complexes using PELDOR distance measurements for rigid body minimisation experiments using XPLOR-NIH. In: Methods. 2014 ; Vol. 70, No. 2-3. pp. 139-53.

Bibtex

@article{b037feebf1e345728a09f5bd1ea97f17,
title = "Modelling multi-protein complexes using PELDOR distance measurements for rigid body minimisation experiments using XPLOR-NIH",
abstract = "Crystallographic and NMR approaches have provided a wealth of structural information about protein domains. However, often these domains are found as components of larger multi domain polypeptides or complexes. Orienting domains within such contexts can provide powerful new insight into their function. The combination of site specific spin labelling and Pulsed Electron Double Resonance (PELDOR) provide a means of obtaining structural measurements that can be used to generate models describing how such domains are oriented. Here we describe a pipeline for modelling the location of thio-reactive nitroxyl spin locations to engineered sties on the histone chaperone Vps75. We then use a combination of experimentally determined measurements and symmetry constraints to model the orientation in which homodimers of Vps75 associate to form homotetramers using the XPLOR-NIH platform. This provides a working example of how PELDOR measurements can be used to generate a structural model.",
keywords = "Computational Biology, Electron Spin Resonance Spectroscopy, Histone Chaperones, Models, Molecular, Software, Spin Labels, Journal Article, Research Support, Non-U.S. Gov't",
author = "Hammond, {Colin M} and Tom Owen-Hughes and Norman, {David G}",
note = "Copyright {\textcopyright} 2014 The Authors. Published by Elsevier Inc. All rights reserved.",
year = "2014",
month = dec,
doi = "10.1016/j.ymeth.2014.10.028",
language = "English",
volume = "70",
pages = "139--53",
journal = "Methods",
issn = "1046-2023",
publisher = "Academic Press",
number = "2-3",

}

RIS

TY - JOUR

T1 - Modelling multi-protein complexes using PELDOR distance measurements for rigid body minimisation experiments using XPLOR-NIH

AU - Hammond, Colin M

AU - Owen-Hughes, Tom

AU - Norman, David G

N1 - Copyright © 2014 The Authors. Published by Elsevier Inc. All rights reserved.

PY - 2014/12

Y1 - 2014/12

N2 - Crystallographic and NMR approaches have provided a wealth of structural information about protein domains. However, often these domains are found as components of larger multi domain polypeptides or complexes. Orienting domains within such contexts can provide powerful new insight into their function. The combination of site specific spin labelling and Pulsed Electron Double Resonance (PELDOR) provide a means of obtaining structural measurements that can be used to generate models describing how such domains are oriented. Here we describe a pipeline for modelling the location of thio-reactive nitroxyl spin locations to engineered sties on the histone chaperone Vps75. We then use a combination of experimentally determined measurements and symmetry constraints to model the orientation in which homodimers of Vps75 associate to form homotetramers using the XPLOR-NIH platform. This provides a working example of how PELDOR measurements can be used to generate a structural model.

AB - Crystallographic and NMR approaches have provided a wealth of structural information about protein domains. However, often these domains are found as components of larger multi domain polypeptides or complexes. Orienting domains within such contexts can provide powerful new insight into their function. The combination of site specific spin labelling and Pulsed Electron Double Resonance (PELDOR) provide a means of obtaining structural measurements that can be used to generate models describing how such domains are oriented. Here we describe a pipeline for modelling the location of thio-reactive nitroxyl spin locations to engineered sties on the histone chaperone Vps75. We then use a combination of experimentally determined measurements and symmetry constraints to model the orientation in which homodimers of Vps75 associate to form homotetramers using the XPLOR-NIH platform. This provides a working example of how PELDOR measurements can be used to generate a structural model.

KW - Computational Biology

KW - Electron Spin Resonance Spectroscopy

KW - Histone Chaperones

KW - Models, Molecular

KW - Software

KW - Spin Labels

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1016/j.ymeth.2014.10.028

DO - 10.1016/j.ymeth.2014.10.028

M3 - Journal article

C2 - 25448300

VL - 70

SP - 139

EP - 153

JO - Methods

JF - Methods

SN - 1046-2023

IS - 2-3

ER -

ID: 178883149