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Literature DB >> 2672452

How does protein folding get started?

Abstract

Three models for the initiation of protein folding are considered in the light of recent experiments. The three models emphasize the possible roles of: (1) a hydrophobic collapse, (2) formation of secondary structure, or (3) formation of one or more specific interactions. Whether these models are likely to be contradictory or complementary is discussed.

Mesh：
Protein Conformation

Year: 1989 PMID： 2672452 DOI： 10.1016/0968-0004(89)90067-4

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

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Cited

33 in total

1. An engineered leucine zipper a position mutant with an unusual three-state unfolding pathway.

Authors: H Zhu; S A Celinski; J M Scholtz; J C Hu
Journal: Protein Sci Date: 2001-01 Impact factor: 6.725

2. Folding propensities of synthetic peptide fragments covering the entire sequence of phage 434 Cro protein.

Authors: S Padmanabhan; M A Jiménez; M Rico
Journal: Protein Sci Date: 1999-08 Impact factor: 6.725

3. Ultrafast folding of alpha3D: a de novo designed three-helix bundle protein.

Authors: Yongjin Zhu; Darwin O V Alonso; Kosuke Maki; Cheng-Yen Huang; Steven J Lahr; Valerie Daggett; Heinrich Roder; William F DeGrado; Feng Gai
Journal: Proc Natl Acad Sci U S A Date: 2003-12-11 Impact factor: 11.205

4. Interatomic potentials and solvation parameters from protein engineering data for buried residues.

Authors: Andrei L Lomize; Mikhail Y Reibarkh; Irina D Pogozheva
Journal: Protein Sci Date: 2002-08 Impact factor: 6.725

Review 5. Protein folding.

Authors: T E Creighton
Journal: Biochem J Date: 1990-08-15 Impact factor: 3.857

How does protein folding get started?

1. An engineered leucine zipper a position mutant with an unusual three-state unfolding pathway.

2. Folding propensities of synthetic peptide fragments covering the entire sequence of phage 434 Cro protein.

3. Ultrafast folding of alpha3D: a de novo designed three-helix bundle protein.

4. Interatomic potentials and solvation parameters from protein engineering data for buried residues.

Review 5. Protein folding.

6. Removal of N-glycosylation sites of the yeast acid phosphatase severely affects protein folding.

Review 7. Implications of aromatic-aromatic interactions: From protein structures to peptide models.

8. Endoplasmic reticulum-associated degradation of the renal potassium channel, ROMK, leads to type II Bartter syndrome.

9. Protein folding: are we there yet?

10. Conformational isomers of denatured and unfolded proteins: methods of production and applications.