Membrane protein folding and stability

Otzen, Daniel E.

doi:10.1016/j.abb.2014.10.014

Cited by 5 publications

(5 citation statements)

References 5 publications

(5 reference statements)

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“…49 The position of aromatic residues in the helices is also a rate-limiting step in membrane insertion: they are considered less favorable when placed centrally and become energetically favorable when moved apart. [50][51][52][53] Tamm, Kleinschmidt, and co-workers were the first to investigate the role of aromatic interactions in the folding and stability of integral b-barrel membrane proteins. [54][55][56][57] Using the bacterial outer membrane protein A as their model, the Tamm group observed that aromatic side chains can form a girdle and interact with each other even if they are 7 Å apart ( Fig.…”

Section: Similarities and Differences In Aromatics Of Soluble And Memmentioning

confidence: 99%

“…Tryptophan, in particular, also acts as stop‐transfer sequences during co‐translational folding of these proteins in the membrane . The position of aromatic residues in the helices is also a rate‐limiting step in membrane insertion: they are considered less favorable when placed centrally and become energetically favorable when moved apart …”

Section: Similarities and Differences In Aromatics Of Soluble And Mem...mentioning

confidence: 99%

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Implications of aromatic–aromatic interactions: From protein structures to peptide models

2015

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With increasing structural information on proteins, the opportunity to understand physical forces governing protein folding is also expanding. One of the significant non-covalent forces between the protein side chains is aromatic-aromatic interactions. Aromatic interactions have been widely exploited and thoroughly investigated in the context of folding, stability, molecular recognition, and self-assembly processes. Through this review, we discuss the contribution of aromatic interactions to the activity and stability of thermophilic, mesophilic, and psychrophilic proteins. Being hydrophobic, aromatic amino acids tend to reside in the protein hydrophobic interior or transmembrane segments of proteins. In such positions, it can play a diverse role in soluble and membrane proteins, and in a-helix and b-sheet stabilization. We also highlight here some excellent investigations made using peptide models and several approaches involving arylaryl interactions, as an increasingly popular strategy in protein and peptide engineering. A recent survey described the existence of aromatic clusters (trimer, tetramer, pentamer, and higher order assemblies), revealing the self-associating property of aryl groups, even in folded protein structures. The application of this self-assembly of aromatics in the generation of modern bionanomaterials is also discussed.

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Section: Similarities and Differences In Aromatics Of Soluble And Memmentioning

confidence: 99%

Section: Similarities and Differences In Aromatics Of Soluble And Mem...mentioning

confidence: 99%

Implications of aromatic–aromatic interactions: From protein structures to peptide models

2015

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“…The results showed that for most of the E. coli , the expression of PagP enzyme after adding mutant was lower than with antibacterial peptide LL-37, while the expression of PagP enzyme after adding antibacterial peptide LL-37 was higher than without antimicrobial peptides. Reports showed that the alkyl acyltransferase PagP of the outer membrane of gram-negative bacteria cells can transfer a fatty acid chain with 16 carbons from phospholipid to β2 position of lipoid A, producing 7 lipoid A with the structure of fatty acid chain, which could disturb the recognition of host immune cell TLR-4 on lipid A, at the same time, lead to its resistance to antimicrobial peptide [ 16 , 17 ]. Therefore, antibacterial peptide LL-37 could stimulate the production of PagP, and increase the expression of PagP.…”

Section: Discussionmentioning

confidence: 99%

Escherichia coli PagP Enzyme-Based De Novo Design and In Vitro Activity of Antibacterial Peptide LL-37

et al. 2017

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BackgroundThe aim of this study was to investigate the antimicrobial property of peptide LL-37 sequences.Material/MethodsHumanized antibacterial peptide LL-37 and the mutant were prepared by chemical synthesis. The physicochemical properties of antibacterial peptide LL-37 were analyzed by SWISS-MODEL online prediction tool. Molecular docking between antibacterial peptide LL-37 fragments and palmitoyl transferase PagP was made with Lamarckian genetic algorithm by AutoDock1.5.6.ResultsThe systems contacted each other at 8.75 picosec. After 20 picsec, the system had no trend of dissociation, and the bond energy of weak bond -C-O-H…NH2-CH2- was calculated. The hydrophobic groups were important factors that led to contact and merged the two parts. The contacted weak bond -C-O-H…NH2-CH2- was the bridge for contacting LL-37 with palmitoyl transferase PagP. The binding sites of antibacterial peptide LL-37 and palmitoyl transferase PagP mainly included LYS8, GLU11, LEU28, LYS12, PHE27, ILE13, and PHE6 of antibacterial peptide LL-37 and ARG94, TRP89, ASN65, SER3, GLU90, GLU90, ASN100, HIS102, and THR92 of palmitoyl transferase PagP.ConclusionsAntibacterial peptide LL-37 had stronger antibacterial effect via inhibition of activity of PagP.

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“…Currently, lipids in the form of nanodiscs and liposomes can be used to stabilize membrane proteins for both structural and functional analysis [ 20 , 21 , 22 , 23 ]. The progress in the development of experimental techniques influences and makes possible the application of theoretical investigations, including the simulation of molecular dynamics [ 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 ]. Accessibility to a permanently grooving database of membrane proteins makes this research easier and more fruitful [ 33 ].…”

Section: Introductionmentioning

confidence: 99%

Connexins and Pannexins—Similarities and Differences According to the FOD-M Model

et al. 2022

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Connexins and pannexins are the transmembrane proteins of highly distinguished biological activity in the form of transport of molecules and electrical signals. Their common role is to connect the external environment with the cytoplasm of the cell, while connexin is also able to link two cells together allowing the transport from one to another. The analysis presented here aims to identify the similarities and differences between connexin and pannexin. As a comparative criterion, the hydrophobicity distribution in the structure of the discussed proteins was used. The comparative analysis is carried out with the use of a mathematical model, the FOD-M model (fuzzy oil drop model in its Modified version) expressing the specificity of the membrane’s external field, which in the case of the discussed proteins is significantly different from the external field for globular proteins in the polar environment of water. The characteristics of the external force field influence the structure of protein allowing the activity in a different environment.

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Membrane protein folding and stability

Cited by 5 publications

References 5 publications

Implications of aromatic–aromatic interactions: From protein structures to peptide models

Implications of aromatic–aromatic interactions: From protein structures to peptide models

Escherichia coli PagP Enzyme-Based De Novo Design and In Vitro Activity of Antibacterial Peptide LL-37

Connexins and Pannexins—Similarities and Differences According to the FOD-M Model

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