期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 57, 期 52, 页码 17194-17199出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201812018
关键词
conformation analysis; immunoglobulin; ion mobility; mass spectrometry; molecular dynamics
资金
- London Interdisciplinary Biosciences Consortium (LIDo) BBSRC Doctoral Training Partnership [BB/M009513/1]
- Wellcome Trust [109854/Z/15/Z]
- Waters
- BBSRC [1622063] Funding Source: UKRI
- MRC [G1100090, G0501494, G0200486] Funding Source: UKRI
- Wellcome Trust [109854/Z/15/Z] Funding Source: Wellcome Trust
Immunoglobulins are biomolecules involved in defence against foreign substances. Flexibility is key to their functional properties in relation to antigen binding and receptor interactions. We have developed an integrative strategy combining ion mobility mass spectrometry (IM-MS) with molecular modelling to study the conformational dynamics of human IgG antibodies. Predictive models of all four human IgG subclasses were assembled and their dynamics sampled in the transition from extended to collapsed state during IM-MS. Our data imply that this collapse of IgG antibodies is related to their intrinsic structural features, including Fab arm flexibility, collapse towards the Fc region, and the length of their hinge regions. The workflow presented here provides an accurate structural representation in good agreement with the observed collision cross section for these flexible IgG molecules. These results have implications for studying other nonglobular flexible proteins.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据