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Biochemistry (Moscow)

, Volume 79, Issue 13, pp 1483–1514 | Cite as

How membrane surface affects protein structure

  • V. E. BychkovaEmail author
  • L. V. Basova
  • V. A. Balobanov
Review

Abstract

The immediate environment of the negatively charged membrane surface is characterized by decreased dielectric constant and pH value. These conditions can be modeled by water-alcohol mixtures at moderately low pH. Several globular proteins were investigated under these conditions, and their conformational behavior in the presence of phospholipid membranes was determined, as well as under conditions modeling the immediate environment of the membrane surface. These proteins underwent conformational transitions from the native to a molten globule-like state. Increased flexibility of the protein structure facilitated protein functioning. Our experimental data allow understanding forces that affect the structure of a protein functioning near the membrane surface (in other words, in the membrane field). Similar conformational states are widely reported in the literature. This indicates that the negatively charged membrane surface can serve as a moderately denaturing agent in the cell. We conclude that the effect of the membrane field on the protein structure must be taken into account.

Key words

anionic phospholipid membranes simple alcohols as a model globular proteins apo- and holomyoglobins apo- and holocytochromes c cytochrome b5 human α-lactalbumin conformational changes non-native protein states membrane-protein interactions pathways membrane field 

Abbreviations

apoCyt c

apoform of cytochrome c

apoHLA

Ca2+-free form of human α-lactalbumin

apoMb

apomyoglobin

CD

circular dichroism

Cp.exc

partial excess heat capacity

Cyt b5

cytochrome b 5

DPPC

1,2-dipalmitoyl-3-phosphatidylcholine

DPPG

1,2-dipalmitoyl-3-phosphatidylglycerol

ER

endoplasmic reticulum

GuHCl

guanidinium hydrochloride

holoCyt c

cytochrome c with bound heme

holoMb

myoglobin with bound heme

I

intermediate state

ImaxFl

fluorescence intensity at fluorescence spectrum maximum

iPrOH

isopropanol

LUV

anionic large bilayer vesicles

MeOH

methanol

MG

molten globule state

MIC

micelles of anionic lysoPhL

N

native state

Na-P

mixture of Na-phosphates

NMR

nuclear magnetic resonance

PhL

phospholipid

POPG

1-palmitoyl-2-oleylphosphatidylglycerol

Pr

protein

PS

phosphatidylserine

RBP

retinol-binding protein

SUV

anionic small bilayer vesicles

tBuOH

tret-butanol

U

completely unfolded state

UV

ultraviolet

ΔH

enthalpy change

ɛeff

effective dielectric constant of a medium

λmaxFl

wavelength of fluorescence spectrum maximum

θ

ellipticity

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Copyright information

© Pleiades Publishing, Ltd. 2014

Authors and Affiliations

  • V. E. Bychkova
    • 1
    Email author
  • L. V. Basova
    • 1
  • V. A. Balobanov
    • 1
  1. 1.Institute of Protein ResearchRussian Academy of SciencesPushchino, Moscow RegionRussia

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