Lipid-protein systems paly curtail roles in living systems [49]. Hence, a determination
of their structure at different levels of organization is still one of the most
important tasks in many research projects. A study of lipid-protein systems is based
on many physicochemical techniques, such as spectroscopy of FTIR, Raman, fluorescence,
NMR, EPR, as well as DLS, DSC and TEM methods. In the presented
paper tow of the most frequently used methods, that is FTIR and fluorescence
spectroscopy, will be discussed in details. They are characterized by a relatively low
cost of sample preparation, a short measuring time, and they give a huge number
of structural and physicochemical information about lipid-protein systems. In the
FTIR-ATR spectroscopy many of vibrational bands are commonly used as very precise
vibrational indicators of structural changes in lipids and proteins (Fig. 1) [1–6].
They allows to characterize lipid and protein components separately in mixed systems.
Additionally, structural changes in lipid membranes can be monitored in one
FTIR-ATR experiment simultaneously in a region of hydrophilic lipid head-groups
(Fig. 5) [17, 18], in a hydrophobic part composed of hydrocarbon lipid chains (see
Figures 2 and 3) [7–9], and in a lipid membrane interface represented by ester lipid
groups (Fig. 4) [4, 6, 11, 12]. A secondary structure of proteins and peptides in different
experimental conditions can be defined in the FTIR-ATR spectroscopy on the
base of amide I bands (Fig. 6 and Tabs 1, 2 and 3) [20–22]. A fluorescence spectroscopy
is a complementary methods to FTIR spectroscopy in a study of lipid-protein
systems. It competes information about time-dependent and very fast (in a scale
of femtoseconds) structural processes in both lipids [41–45] and proteins [23, 27,
48]. The folding, denaturation, and aggregation of proteins and lipid membranes
accompanied by changes in an order, packing and hydration of the system under
study [23, 27, 41–45, 48].
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