Aggregation-Prone Near-Native Intermediate Formation during Unfolding of a Structurally Similar Nonlenticular βγ-Crystallin Domain-Reference-Cited by-同舟云学术

Aggregation-Prone Near-Native Intermediate Formation during Unfolding of a Structurally Similar Nonlenticular βγ-Crystallin Domain

Published:2012-10-18 Issue:43 Volume:51 Page:8502-8513
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Rajanikanth V.¹,Srivastava Shanti Swaroop¹,Singh Aditya K.¹,Rajyalakshmi M.¹,Chandra Kousik²,Aravind Penmatsa¹,Sankaranarayanan Rajan¹,Sharma Yogendra¹

Affiliation:

1. Centre for Cellular and Molecular Biology (CCMB), Council of Scientific and Industrial Research (CSIR), Uppal Road, Hyderabad 500 007, India

2. Chemical Science Division, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai, India

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300844u

Reference48 articles.

1. What lessons can be learned from studying the folding of homologous proteins?

2. Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway

3. Structurally Homologous All β-Barrel Proteins Adopt Different Mechanisms of Folding

4. The domains in γb-crystallin: identical fold-different stabilities

5. The family feud: do proteins with similar structures fold via the same pathway?

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