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Literature DB >> 8413599

Peptide engineering. Catalytic molten globules.

W F DeGrado.

Abstract

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Year: 1993 PMID： 8413599 DOI： 10.1038/365488a0

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

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7 in total

1. Rational design of nascent metalloenzymes.

Authors: D E Benson; M S Wisz; H W Hellinga
Journal: Proc Natl Acad Sci U S A Date: 2000-06-06 Impact factor: 11.205

2. An enzymatic molten globule: efficient coupling of folding and catalysis.

Authors: Katherina Vamvaca; Beat Vögeli; Peter Kast; Konstantin Pervushin; Donald Hilvert
Journal: Proc Natl Acad Sci U S A Date: 2004-08-20 Impact factor: 11.205

3. Foldability of a Natural De Novo Evolved Protein.

Authors: Dixie Bungard; Jacob S Copple; Jing Yan; Jimmy J Chhun; Vlad K Kumirov; Scott G Foy; Joanna Masel; Vicki H Wysocki; Matthew H J Cordes
Journal: Structure Date: 2017-10-12 Impact factor: 5.006

4. Loosely-packed dynamical structures with partially-melted surface being the key for thermophilic argonaute proteins achieving high DNA-cleavage activity.

Authors: Lirong Zheng; Hui Lu; Bing Zan; Song Li; Hao Liu; Zhuo Liu; Juan Huang; Yongjia Liu; Fan Jiang; Qian Liu; Yan Feng; Liang Hong
Journal: Nucleic Acids Res Date: 2022-07-22 Impact factor: 19.160

Peptide engineering. Catalytic molten globules.

1. Rational design of nascent metalloenzymes.

2. An enzymatic molten globule: efficient coupling of folding and catalysis.

3. Foldability of a Natural De Novo Evolved Protein.

4. Loosely-packed dynamical structures with partially-melted surface being the key for thermophilic argonaute proteins achieving high DNA-cleavage activity.

5. Mutational analysis of the leucine zipper motif in the Newcastle disease virus fusion protein.

6. The relationship between folding and activity in UreG, an intrinsically disordered enzyme.

7. Roles in cell-to-cell fusion of two conserved hydrophobic regions in the murine coronavirus spike protein.