Tertiary Structure Stabilization Promotes Hairpin Ribozyme Ligation†

Biochemistry ◽  
1999 ◽  
Vol 38 (34) ◽  
pp. 11040-11050 ◽  
Author(s):  
Martha J. Fedor
Keyword(s):  
Tertiary Structure ◽  
Hairpin Ribozyme ◽  
Structure Stabilization

scholarly journals Protein Macrocyclization for Tertiary Structure Stabilization

ChemBioChem ◽  
2021 ◽  
Author(s):  
Anissa Haim ◽  
Saskia Neubacher ◽  
Tom N. Grossmann
Keyword(s):  
Tertiary Structure ◽  
Structure Stabilization

scholarly journals Cooperative RNA Folding under Cellular Conditions Arises From Both Tertiary Structure Stabilization and Secondary Structure Destabilization

Biochemistry ◽  
2017 ◽  
Vol 56 (27) ◽  
pp. 3422-3433 ◽  
Author(s):  
Kathleen A. Leamy ◽  
Neela H. Yennawar ◽  
Philip C. Bevilacqua
Keyword(s):  
Secondary Structure ◽  
Rna Folding ◽  
Tertiary Structure ◽  
Structure Stabilization

scholarly journals Structural modeling and thermostability of a serine protease inhibitor belonging to the Kunitz family from the tick Rhipicephalus microplus

2020 ◽  
Author(s):  
Lívia de Moraes Bomediano Camillo ◽  
Graziele Cristina Ferreira ◽  
Adriana Feliciano Alves Duran ◽  
Flavia Ribeiro Santos da Silva ◽  
Wanius Garcia ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Disulfide Bonds ◽  
Tertiary Structure ◽  
Dissociation Constants ◽  
Serine Protease Inhibitor ◽  
Rhipicephalus Microplus ◽  
Human Neutrophil Elastase ◽  
Structure Stabilization

ABSTRACTrBmTI-A is a recombinant serine protease inhibitor that belongs to the Kunitz-BPTI family and that was cloned from Rhipicephalus microplus tick. rBmTI-A has inhibitory activities on bovine trypsin, human plasma kallikrein, human neutrophil elastase and plasmin with dissociation constants in nM range. It is characterized by two inhibitory domains and each domain presents six cysteines that form three disulfide bonds, which contribute to the high stability of its structure. Previous studies suggest that serine protease inhibitor rBmTI-A has a protective potential against pulmonary emphysema in mice and anti-inflammatory potential, besides rBmTI-A presented a potent inhibitory activity against in vitro vessel formation. In this study, the tertiary structure of BmTI-A was modeled based on the structure of its Sabellastarte magnifica homologue. The structure stabilization was evaluated by molecular dynamics analysis. Circular dichroism data corroborated the secondary structure found by the homology modeling. Thermostability analysis confirmed the thermostability and the relation between the effects of the temperature in the inhibitor activity. The loss of activity observed was gradual, and, after 60 minutes of incubation at 90°C the inhibitor lost it completely.

Tertiary Structure Stability of the Hairpin Ribozyme in Its Natural and Minimal Forms:  Different Energetic Contributions from a Ribose Zipper Motif†

Biochemistry ◽  
2001 ◽  
Vol 40 (37) ◽  
pp. 11211-11218 ◽  
Author(s):  
Dagmar Klostermeier ◽  
David P. Millar
Keyword(s):  
Tertiary Structure ◽  
Structure Stability ◽  
Hairpin Ribozyme
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