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

[ Vol. 17 , Issue. 4 ]

Author(s):

Eugene A. Permyakov, Serge E. Permyakov, Leonid Breydo, Elrashdy M. Redwan, Hussein A. Almehdar and Vladimir N. Uversky   Pages 352 - 367 ( 16 )

Abstract:


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.

Affiliation:

Eugene A. Permyakov, Institute for Biological Instrumentation of the Russian Academy of Sciences, Institutskaya str., 7, Pushchino, Moscow region 142290, Russia., Department of Molecular Medicine, College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd, MDC3540, Tampa, FL 33612, USA.



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