Thermodynamic Analysis of Weak Protein Interactions Using Sedimentation Equilibrium

Overview

Journal Curr Protoc Protein Sci

Specialties Biochemistry
Pathology

Date 2014 Aug 2

PMID 25081741

Citations 4

Authors

Yuri V Sergeev

Monika B Dolinska

Paul T Wingfield

Affiliations

Soon will be listed here.

Abstract

Proteins self-associate to form dimers and tetramers. Purified proteins are used to study the thermodynamics of protein interactions using the analytical ultracentrifuge. In this approach, monomer-dimer equilibrium constants are directly measured at various temperatures. Data analysis is used to derive thermodynamic parameters, such as Gibbs free energy, enthalpy, and entropy, which can predict which major forces are involved in protein association.

Citing Articles

Molecular docking analysis of human JAK2 with compounds from tomatoes.

Vidhya Rekha U, Anita M, Bhuminathan S, Sadhana K Bioinformation. 2021; 16(10):742-747.

PMID: 34675459 PMC: 8503773. DOI: 10.6026/97320630016742.

Characterization of Temperature-Dependent Kinetics of Oculocutaneous Albinism-Causing Mutants of Tyrosinase.

Wachamo S, Patel M, Varghese P, Dolinska M, Sergeev Y Int J Mol Sci. 2021; 22(15).

PMID: 34360537 PMC: 8346126. DOI: 10.3390/ijms22157771.

Human Tyrosinase: Temperature-Dependent Kinetics of Oxidase Activity.

Young II K, Kassouf C, Dolinska M, Anderson D, Sergeev Y Int J Mol Sci. 2020; 21(3).

PMID: 32019134 PMC: 7037427. DOI: 10.3390/ijms21030895.

Enthalpy-Driven Stabilization of Transthyretin by AG10 Mimics a Naturally Occurring Genetic Variant That Protects from Transthyretin Amyloidosis.

Miller M, Pal A, Albusairi W, Joo H, Pappas B, Tuhin M J Med Chem. 2018; 61(17):7862-7876.

PMID: 30133284 PMC: 6276790. DOI: 10.1021/acs.jmedchem.8b00817.

References

Bloemendal H, de Jong W . Lens proteins and their genes. Prog Nucleic Acid Res Mol Biol. 1991; 41:259-81. DOI: 10.1016/s0079-6603(08)60012-4. View

Slingsby C, Bateman O . Quaternary interactions in eye lens beta-crystallins: basic and acidic subunits of beta-crystallins favor heterologous association. Biochemistry. 1990; 29(28):6592-9. DOI: 10.1021/bi00480a007. View

Wistow G, Turnell B, Summers L, Slingsby C, Moss D, Miller L . X-ray analysis of the eye lens protein gamma-II crystallin at 1.9 A resolution. J Mol Biol. 1983; 170(1):175-202. DOI: 10.1016/s0022-2836(83)80232-0. View

Ross P, Subramanian S . Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry. 1981; 20(11):3096-102. DOI: 10.1021/bi00514a017. View

Gill S, von Hippel P . Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem. 1989; 182(2):319-26. DOI: 10.1016/0003-2697(89)90602-7. View

Dolinska M, Sergeev Y, Chan M, Palmer I, Wingfield P . N-terminal extension of beta B1-crystallin: identification of a critical region that modulates protein interaction with beta A3-crystallin. Biochemistry. 2009; 48(40):9684-95. PMC: 2764403. DOI: 10.1021/bi9013984. View

Sergeev Y, Chirgadze Y, Mylvaganam S, Driessen H, Slingsby C, Blundell T . Surface interactions of gamma-crystallins in the crystal medium in relation to their association in the eye lens. Proteins. 1988; 4(2):137-47. DOI: 10.1002/prot.340040207. View

Chan M, Dolinska M, Sergeev Y, Wingfield P, Hejtmancik J . Association properties of betaB1- and betaA3-crystallins: ability to form heterotetramers. Biochemistry. 2008; 47(42):11062-9. PMC: 2752815. DOI: 10.1021/bi8012438. View

Sergeev Y, Wingfield P, Hejtmancik J . Monomer-dimer equilibrium of normal and modified beta A3-crystallins: experimental determination and molecular modeling. Biochemistry. 2000; 39(51):15799-806. DOI: 10.1021/bi001882h. View

10.

Lampi K, Oxford J, Bachinger H, Shearer T, David L, Kapfer D . Deamidation of human beta B1 alters the elongated structure of the dimer. Exp Eye Res. 2001; 72(3):279-88. DOI: 10.1006/exer.2000.0950. View

11.

Lubsen N, Aarts H, Schoenmakers J . The evolution of lenticular proteins: the beta- and gamma-crystallin super gene family. Prog Biophys Mol Biol. 1988; 51(1):47-76. DOI: 10.1016/0079-6107(88)90010-7. View

12.

Iyer K, Klee W . Direct spectrophotometric measurement of the rate of reduction of disulfide bonds. The reactivity of the disulfide bonds of bovine -lactalbumin. J Biol Chem. 1973; 248(2):707-10. View

13.

Dolinska M, Wingfield P, Sergeev Y . βB1-crystallin: thermodynamic profiles of molecular interactions. PLoS One. 2012; 7(1):e29227. PMC: 3253074. DOI: 10.1371/journal.pone.0029227. View

14.

Sergeev Y, Hejtmancik J, Wingfield P . Energetics of domain-domain interactions and entropy driven association of beta-crystallins. Biochemistry. 2004; 43(2):415-24. DOI: 10.1021/bi034617f. View

15.

Takata T, Woodbury L, Lampi K . Deamidation alters interactions of beta-crystallins in hetero-oligomers. Mol Vis. 2009; 15:241-9. PMC: 2633459. View

16.

Willoughby C, Shafiq A, Ferrini W, Chan L, Billingsley G, Priston M . CRYBB1 mutation associated with congenital cataract and microcornea. Mol Vis. 2005; 11:587-93. View

17.

Bax B, Lapatto R, Nalini V, Driessen H, Lindley P, Mahadevan D . X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins. Nature. 1990; 347(6295):776-80. DOI: 10.1038/347776a0. View