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Disorder in milk proteins: caseins, intrinsically disordered colloids
Elrashdy M Redwan, Bin Xue, Hussein A Almehdar
1Department of Biological Science, Faculty of Science, King Abdulaziz University, Jeddah, PO Box 80203, Jeddah 21589, Saudi Arabia. vuversky@health.usf.edu.
Current Protein & Peptide Science
|February 26, 2015
Summary
Caseins, abundant milk proteins, exhibit intrinsic disorder crucial for their diverse functions, including nutrient transport and health benefits. This review explores how their amino acid sequences encode this disorder.
Area of Science:
- Biochemistry
- Proteomics
- Molecular Biology
Background:
- Caseins are the most abundant and extensively studied milk proteins.
- They are known for their intrinsically disordered nature, influencing their functions.
- Casein's disorder is key to its roles in nutrition, calcium transport, and health.
Purpose of the Study:
- To review the abundance and roles of intrinsic disorder in milk proteins, focusing on caseins.
- To explore how intrinsic disorder is encoded within casein amino acid sequences.
- To highlight casein's diverse functions, from nutritional to protective.
Main Methods:
- Literature review of intrinsic disorder in milk proteins.
- Analysis of casein structure-function relationships.
- Examination of amino acid sequence determinants of intrinsic disorder.
Main Results:
- Caseins (αs1-, αs2-, β-, κ-caseins) are highly disordered proteins.
- Intrinsic disorder underpins casein's roles in calcium phosphate transport and micelle formation.
- Disordered nature contributes to nutritional, chaperone, and protective functions.
Conclusions:
- Intrinsic disorder is a fundamental property of caseins, essential for their biological and industrial functions.
- Understanding the sequence basis of casein disorder is crucial for elucidating their roles.
- Caseins serve as a model for studying functional intrinsically disordered proteins.
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