Dynamics and mechanisms of coupled protein folding and binding reactions

T Kiefhaber, A Bachmann, KS Jensen - Current opinion in structural biology, 2012 - Elsevier
Protein folding coupled to binding of a specific ligand is frequently observed in biological
processes. In recent years numerous studies have addressed the structural properties of the …

Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins

M Arai - Biophysical reviews, 2018 - Springer
Extensive experimental and theoretical studies have advanced our understanding of the
mechanisms of folding and binding of globular proteins, and coupled folding and binding of …

Dilute phase oligomerization can oppose phase separation and modulate material properties of a ribonucleoprotein condensate

I Seim, AE Posey, WT Snead… - Proceedings of the …, 2022 - National Acad Sciences
Ribonucleoprotein bodies are exemplars of membraneless biomolecular condensates that
can form via spontaneous or driven phase transitions. The fungal protein Whi3 forms …

Equilibrium thermal transitions of collagen model peptides

AV Persikov, Y Xu, B Brodsky - Protein Science, 2004 - Wiley Online Library
The folding of collagen in vitro is very slow and presents difficulties in reaching equilibrium,
a feature that may have implications for in vivo collagen function. Peptides serve as good …

Nucleation and propagation of the collagen triple helix in single-chain and trimerized peptides: transition from third to first order kinetics

S Boudko, S Frank, RA Kammerer, J Stetefeld… - Journal of molecular …, 2002 - Elsevier
The kinetics of triple helix formation from single non-crosslinked peptide chains were studied
for the collagen models (ProProGly) 10 and (ProHypGly) 10 in a broad concentration range …

Structure and dynamics of the Human multi-tRNA synthetase complex

MH Kim, BS Kang - Macromolecular Protein Complexes IV: Structure and …, 2022 - Springer
Aminoacyl-tRNA synthetases (ARSs) are essential enzymes that ligate amino acids to their
cognate tRNAs during protein synthesis. A growing body of scientific evidence …

Hg (II) binding to a weakly associated coiled coil nucleates an encoded metalloprotein fold: A kinetic analysis

BT Farrer, VL Pecoraro - Proceedings of the National …, 2003 - National Acad Sciences
A detailed kinetic analysis of metal encapsulation by a de novo-designed protein is
described. The kinetic mechanism of Hg (II) encapsulation in the three-stranded coiled coil …

Kinetics and thermodynamics of the unfolding and refolding of the three-stranded α-helical coiled coil, Lpp-56

AI Dragan, SA Potekhin, A Sivolob, M Lu… - Biochemistry, 2004 - ACS Publications
Temperature-induced reversible unfolding and refolding of the three-stranded α-helical
coiled coil, Lpp-56, were studied by kinetic and thermodynamic methods, using CD …

In vivo bypass of chaperone by extended coiled-coil motif in T4 tail fiber

Y Qu, P Hyman, T Harrah, E Goldberg - Journal of bacteriology, 2004 - Am Soc Microbiol
The distal-half tail fiber of bacteriophage T4 is made of three gene products: trimeric gp36
and gp37 and monomeric gp35. Chaperone P38 is normally required for folding gp37 …

[HTML][HTML] Structural polymorphism of coiled‐coils from the stalk domain of SARS‐CoV‐2 spike protein

Z Živič, Ž Strmšek, M Novinec, J Lah, S Hadži - The FASEB Journal, 2022 - ncbi.nlm.nih.gov
Spike trimer plays a key role in SARS‐CoV‐2 infection and vaccine development. It consists
of a globular head and a flexible stalk domain that anchors the protein into the viral …