Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding

2013 ◽  
Vol 20 (7) ◽  
pp. 843-850 ◽  
Author(s):  
Arzu Sandikci ◽  
Felix Gloge ◽  
Michael Martinez ◽  
Matthias P Mayer ◽  
Rebecca Wade ◽  
...  
Keyword(s):  
Polypeptide Folding

scholarly journals Application of evolutionary algorithm methods to polypeptide folding: Comparison with experimental results for unsolvated Ac-(Ala-Gly-Gly)5-LysH+

2004 ◽  
Vol 101 (19) ◽  
pp. 7215-7222 ◽  
Author(s):  
M. Damsbo ◽  
B. S. Kinnear ◽  
M. R. Hartings ◽  
P. T. Ruhoff ◽  
M. F. Jarrold ◽  
...  
Keyword(s):  
Evolutionary Algorithm ◽  
Experimental Results ◽  
Polypeptide Folding

The redox switch that regulates molecular chaperones

2015 ◽  
Vol 6 (4) ◽  
pp. 269-284 ◽  
Author(s):  
Myra E. Conway ◽  
Christopher Lee
Keyword(s):  
Redox Regulation ◽  
Structural Rearrangement ◽  
Antioxidant Systems ◽  
Cysteine Oxidation ◽  
Hydrophobic Region ◽  
Physiological Importance ◽  
Redox Active ◽  
Polypeptide Folding ◽  
Integral Role ◽  
The Impact

AbstractModification of reactive cysteine residues plays an integral role in redox-regulated reactions. Oxidation of thiolate anions to sulphenic acid can result in disulphide bond formation, or overoxidation to sulphonic acid, representing reversible and irreversible endpoints of cysteine oxidation, respectively. The antioxidant systems of the cell, including the thioredoxin and glutaredoxin systems, aim to prevent these higher and irreversible oxidation states. This is important as these redox transitions have numerous roles in regulating the structure/function relationship of proteins. Proteins with redox-active switches as described for peroxiredoxin (Prx) and protein disulphide isomerase (PDI) can undergo dynamic structural rearrangement resulting in a gain of function. For Prx, transition from cysteine sulphenic acid to sulphinic acid is described as an adaptive response during increased cellular stress causing Prx to form higher molecular weight aggregates, switching its role from antioxidant to molecular chaperone. Evidence in support of PDI as a redox-regulated chaperone is also gaining impetus, where oxidation of the redox-active CXXC regions causes a structural change, exposing its hydrophobic region, facilitating polypeptide folding. In this review, we will focus on these two chaperones that are directly regulated through thiol-disulphide exchange and detail how these redox-induced switches allow for dual activity. Moreover, we will introduce a new role for a metabolic protein, the branched-chain aminotransferase, and discuss how it shares common mechanistic features with these well-documented chaperones. Together, the physiological importance of the redox regulation of these proteins under pathological conditions such as Alzheimer’s disease, Parkinson’s disease, and amyotrophic lateral sclerosis will be discussed to illustrate the impact and importance of correct folding and chaperone-mediated activity.

Monte Carlo vs Molecular Dynamics for All-Atom Polypeptide Folding Simulations

2006 ◽  
Vol 110 (33) ◽  
pp. 16733-16742 ◽  
Author(s):  
Jakob P. Ulmschneider ◽  
Martin B. Ulmschneider ◽  
Alfredo Di Nola
Keyword(s):  
Molecular Dynamics ◽  
Monte Carlo ◽  
Polypeptide Folding ◽  
Folding Simulations

A CD strategy for the study of polypeptide folding/unfolding

2009 ◽  
Vol 38 (6) ◽  
pp. 519-527 ◽  
Author(s):  
GIULIANO SILIGARDI ◽  
ALEX F. DRAKE ◽  
PAOLO MASCAGNI ◽  
DAVID J. ROWLANDS ◽  
FRED BROWN ◽  
...  
Keyword(s):  
Polypeptide Folding

scholarly journals Codon bias determines sorting of ion channel protein

2020 ◽  
Author(s):  
Marina Kithil ◽  
Anja Jeannine Engel ◽  
Markus Langhans ◽  
Oliver Rauh ◽  
Matea Cartolano ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Secretory Pathway ◽  
Model Systems ◽  
Dependent Manner ◽  
Intracellular Proteins ◽  
Polypeptide Folding ◽  
A Cell ◽  
Identical Amino Acid Sequence ◽  
Cycle Dependent ◽  
The Impact

AbstractThe choice of codons can influence local translation kinetics during protein synthesis. The question of whether the modulation of polypeptide folding and binding to chaperons influences sorting of nascent membrane proteins remains unclear. Here, we use two similar K+ channels as model systems to examine the impact of codon choice on protein sorting. By monitoring transient expression of GFP tagged proteins in mammalian cells we find that targeting of one channel to the secretory pathway is insensitive to codon optimization. In contrast, sorting of the second channel to the mitochondria is very sensitive to codon choice. The protein with an identical amino acid sequence is sorted in a codon and cell cycle dependent manner either to mitochondria or the secretory pathway. The data establish that a gene with either rare or frequent codons serves together with a cell-state depending decoding mechanism as a secondary code for sorting intracellular proteins.

scholarly journals Engineering polypeptide folding through trans double bonds: transformation of miniature β-meanders to hybrid helices

2015 ◽  
Vol 51 (69) ◽  
pp. 13397-13399 ◽  
Author(s):  
Mothukuri Ganesh Kumar ◽  
Sushil N. Benke ◽  
K. Muruga Poopathi Raja ◽  
Hosahudya N. Gopi
Keyword(s):  
Single Crystal ◽  
Catalytic Hydrogenation ◽  
The Novel ◽  
Double Bonds ◽  
Polypeptide Folding ◽  
P Utilization

Utilization of conjugated double bonds to engineer the novel folded miniature β-meander type structures, transformation of miniature β-meanders into 10/12-helices using catalytic hydrogenation, their solution and single crystal conformations are reported.

Polypeptide Folding-Mediated Tuning of the Optical and Structural Properties of Gold Nanoparticle Assemblies

Nano Letters ◽  
2011 ◽  
Vol 11 (12) ◽  
pp. 5564-5573 ◽  
Author(s):  
Daniel Aili ◽  
Piotr Gryko ◽  
Borja Sepulveda ◽  
John A. G. Dick ◽  
Nigel Kirby ◽  
...  
Keyword(s):  
Gold Nanoparticle ◽  
Structural Properties ◽  
Nanoparticle Assemblies ◽  
Polypeptide Folding
Sign in / Sign up

Export Citation Format

Share Document