منابع مشابه
Kinetic nonoptimality and vibrational stability of proteins.
Scaling of folding times in Go models of proteins and of decoy structures with the Lennard-Jones potentials in the native contacts reveal power law trends when studied under optimal folding conditions. The power law exponent depends on the type of native geometry. Its value indicates lack of kinetic optimality in the model proteins. In proteins, mechanical and thermodynamic stabilities are corr...
متن کاملThermal stability of membrane-bound proteins
nanoDSF, the miniaturized differential scanning fluorimetry technology, is a revolutionary method to determine the thermostability of proteins by following changes in their intrinsic fluorescence. In this comparative study, the Prometheus NT.48 was used to determine the thermal stability of the membrane esterase PA2949 from Pseudomonas aeruginosa in presence of various detergents. The detergent...
متن کاملStability of "salt bridges" in membrane proteins.
We estimate the free energies of transfer of ionized amino acid side chains in water to both their ion-paired and neutral hydrogen-bonded states in low-dielectric media. The difference between the two free energies corresponds to the proton transfer free energy in a "salt bridge" formed between acidic and basic groups (i.e., lysine and glutamic acid residues). Our approach is to use gas phase p...
متن کاملMeasuring the conformational stability of membrane proteins using the UNit
Introduction Use of extrinsic dyes to study protein unfolding Measurement of thermal stability is a valuable tool for assessing the suitability of proteins to a wide range of applications, including their use as therapeutic drugs or food additives. Indeed, researchers commonly require practical methods to rapidly screen conditions that afford the best environment for a particular protein. The U...
متن کاملAssembly and Stability of α-Helical Membrane Proteins.
Grease to grease - this is how one might begin to describe the tendency of hydrophobic stretches in protein amino acid sequences to form transmembrane domains. While this simple rule contains a lot of truth, the mechanisms of membrane protein folding, the insertion of hydrophobic protein domains into the lipid bilayer, and the apparent existence of highly polar residues in some proteins in the ...
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ژورنال
عنوان ژورنال: Biophysical Reviews
سال: 2017
ISSN: 1867-2450,1867-2469
DOI: 10.1007/s12551-017-0324-0