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Literature DB >> 15935679

The membrane-water interface region of membrane proteins: structural bias and the anti-snorkeling effect.

Jie Liang¹, Larisa Adamian, Ronald Jackups.

Abstract

Membrane proteins have important roles in many cellular processes. Computational analysis of their sequences and structures has provided much insight into the organizing principles of transmembrane helices. In a recent study, the membrane-water interface region was examined in detail for the first time. The results have revealed that this interface region has an important role in constraining protein secondary structure. This study raises new questions and opens up new directions for studying membrane proteins.

Entities: Chemical

Mesh：

Substances：
Membrane Proteins
Water

Year: 2005 PMID： 15935679 DOI： 10.1016/j.tibs.2005.05.003

Source DB: PubMed Journal: Trends Biochem Sci ISSN： 0968-0004 Impact factor: 13.807

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Cited

12 in total

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Journal: Biophys J Date: 2009-03-18 Impact factor: 4.033

Review 2. Calcitonin and calcitonin receptor-like receptors: common themes with family B GPCRs?

Authors: James Barwell; Joseph J Gingell; Harriet A Watkins; Julia K Archbold; David R Poyner; Debbie L Hay
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3. Dramatic destabilization of transmembrane helix interactions by features of natural membrane environments.

Authors: Heedeok Hong; James U Bowie
Journal: J Am Chem Soc Date: 2011-07-05 Impact factor: 15.419

4. Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB.

Authors: Kenji Inaba; Yoh-hei Takahashi; Koreaki Ito; Shigehiko Hayashi
Journal: Proc Natl Acad Sci U S A Date: 2005-12-29 Impact factor: 11.205

5. Contribution of topology determinants of a viral movement protein to its membrane association, intracellular traffic, and viral cell-to-cell movement.

Authors: A Genovés; V Pallás; J A Navarro
Journal: J Virol Date: 2011-05-18 Impact factor: 5.103

6. Identification of Tyr residues that enhance folate substrate binding and constrain oscillation of the proton-coupled folate transporter (PCFT-SLC46A1).

Authors: Michele Visentin; Ersin Selcuk Unal; Mitra Najmi; Andras Fiser; Rongbao Zhao; I David Goldman
Journal: Am J Physiol Cell Physiol Date: 2015-01-21 Impact factor: 4.249

The membrane-water interface region of membrane proteins: structural bias and the anti-snorkeling effect.

1. The effect of loops on the structural organization of alpha-helical membrane proteins.

Review 2. Calcitonin and calcitonin receptor-like receptors: common themes with family B GPCRs?

3. Dramatic destabilization of transmembrane helix interactions by features of natural membrane environments.

4. Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB.

5. Contribution of topology determinants of a viral movement protein to its membrane association, intracellular traffic, and viral cell-to-cell movement.

6. Identification of Tyr residues that enhance folate substrate binding and constrain oscillation of the proton-coupled folate transporter (PCFT-SLC46A1).

7. Structural determinant of functionality in acyl lipid desaturases.

8. P-glycoprotein is fully active after multiple tryptophan substitutions.

9. A folding pathway-dependent score to recognize membrane proteins.

10. Prediction of transmembrane helix orientation in polytopic membrane proteins.