Towards understanding the sequence structure function relationship of intrinsically disordered LEA_4 proteins from Arabidopsis thaliana Water deficits can cause lethal damage to organisms which is rooted in cellular dehydration. Many plant species but also other organisms have developed mechanisms to tolerate such stresses such as the expression of LEA proteins. Many studies report on physiological protective functions of LEA proteins but lack information about their precise mechanisms on a molecular level. Most LEA proteins are intrinsically disordered in dilute solution but may adopt a distinct secondary structure upon changes in solvent conditions. Understanding the molecular mechanism of how LEA proteins contribute to the counteraction of cellular damage during water deficits may in the long term pave the way for breeding crops that are resistant to the effects of global warming. The objective of the work at hand is to improve the biophysical understanding of the sequencestructure function relationship of LEA proteins as membrane stabilizers based on the LEA_4 family of the model plant A. thaliana. This is pursued by using a combination of spectroscopic and scattering techniques supported by bioinformatics and computational analyses.