Disorder in Milk Proteins: α -Lactalbumin. Part A. Structural Properties and Conformational Behavior

Author(s): Eugene A. Permyakov, Serge E. Permyakov, Leonid Breydo, Elrashdy M. Redwan, Hussein A. Almehdar, Vladimir N. Uversky

Journal Name: Current Protein & Peptide Science

Volume 17 , Issue 4 , 2016

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This is a first part of the two-part article that continues a series of reviews on the abundance and roles of intrinsic disorder in milk proteins. We introduce here α-lactalbumin, a small (Mr 14 200), simple, acidic (pI 4–5), Ca2+-binding protein that might constitute up to 20% of total milk protein. Although function (it is one of the two components of lactose synthase that catalyzes the final step of the lactose biosynthesis in the lactating mammary gland), structure (protein has two domains, a large α -helical domain and a small β -sheet domain connected by a calcium binding loop), and folding mechanisms (α-lactalbumin is well-known as a classic example of the molten globule state) of this model globular protein are relatively well understood, α-lactalbumin continues to surprise researchers and clearly continues to have high discovery potential. The goal of this review is to summarize some recent advances in the field of α-lactalbumin research and to analyze the peculiarities of the “intrinsic disorder code” of this protein.

Keywords: α-Lactalbumin, molten globule, calcium binding, intrinsic disorder, structure, stability.

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Article Details

Year: 2016
Published on: 04 April, 2016
Page: [352 - 367]
Pages: 16
DOI: 10.2174/138920371704160405001222
Price: $65

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