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Literature DB >> 9019474

Local interactions in protein folding: lessons from the alpha-helix.

R Aurora¹, T P Creamer, R Srinivasan, G D Rose.

Abstract

Mesh：

Year: 1997 PMID： 9019474 DOI： 10.1074/jbc.272.3.1413

Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157

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28 in total

1. A physical basis for protein secondary structure.

Authors: R Srinivasan; G D Rose
Journal: Proc Natl Acad Sci U S A Date: 1999-12-07 Impact factor: 11.205

2. Multiple unfolding intermediates of human placental alkaline phosphatase in equilibrium urea denaturation.

Authors: H C Hung; G G Chang
Journal: Biophys J Date: 2001-12 Impact factor: 4.033

3. Mining combinatorial data in protein sequences and structures.

Authors: S G Jacchieri
Journal: Mol Divers Date: 2000 Impact factor: 2.943

4. Steric restrictions in protein folding: an alpha-helix cannot be followed by a contiguous beta-strand.

Authors: Nicholas C Fitzkee; George D Rose
Journal: Protein Sci Date: 2004-02-06 Impact factor: 6.725

5. Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness.

Authors: Takanori Uzawa; Shuji Akiyama; Tetsunari Kimura; Satoshi Takahashi; Koichiro Ishimori; Isao Morishima; Tetsuro Fujisawa
Journal: Proc Natl Acad Sci U S A Date: 2004-01-07 Impact factor: 11.205

6. Resolution of the effects induced by W → F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F.

Authors: Giuseppe Infusini; Clara Iannuzzi; Silvia Vilasi; Leila Birolo; Daniela Pagnozzi; Piero Pucci; Gaetano Irace; Ivana Sirangelo
Journal: Eur Biophys J Date: 2012-06-22 Impact factor: 1.733

Local interactions in protein folding: lessons from the alpha-helix.

1. A physical basis for protein secondary structure.

2. Multiple unfolding intermediates of human placental alkaline phosphatase in equilibrium urea denaturation.

3. Mining combinatorial data in protein sequences and structures.

4. Steric restrictions in protein folding: an alpha-helix cannot be followed by a contiguous beta-strand.

5. Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness.

6. Resolution of the effects induced by W → F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F.

7. Non-covalent interactions: Fold globally, bond locally.

8. Residue-specific side-chain packing determines the backbone dynamics of transmembrane model helices.

9. The effect of charge-charge interactions on the kinetics of alpha-helix formation.

10. Crystal structure of the transcriptional regulator CmeR from Campylobacter jejuni.