Thermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: case study from bacteria and humans-Reference-Cited by-同舟云学术

Thermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: case study from bacteria and humans

Published:2015 Issue:2 Volume:5 Page:1227-1234
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Gupta Ankit¹²³⁴⁵,Iyer Bharat Ramasubramanian¹²³⁴⁵,Chaturvedi Deepti¹²³⁴⁵,Maurya Svetlana Rajkumar¹²³⁴⁵,Mahalakshmi Radhakrishnan¹²³⁴⁵

Affiliation:

1. Molecular Biophysics Laboratory

2. Department of Biological Sciences

3. Indian Institute of Science Education and Research

4. Bhopal

5. India

Abstract

Purification-free transmembrane protein inclusion body preparations for rapid and cost-effective biophysical, functional and structural studies.

Funder

Science and Engineering Research Board

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/RA/C4RA11207E

Reference71 articles.

1. MEMBRANE PROTEIN ASSEMBLY: GENETIC, EVOLUTIONARY AND MEDICAL PERSPECTIVES

3. Mechanism of Amyloid β-Protein Aggregation Mediated by GM1 Ganglioside Clusters

4. Membrane protein misassembly in disease

5. Structural insights into the transport of small molecules across membranes

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