Side-chain entropy effects on protein secondary structure formation

2005 ◽  
Vol 62 (2) ◽  
pp. 411-420 ◽  
Author(s):  
Brian W. Chellgren ◽  
Trevor P. Creamer
Keyword(s):  
Secondary Structure ◽  
Structure Formation ◽  
Protein Secondary Structure ◽  
Side Chain ◽  
Secondary Structure Formation ◽  
Entropy Effects

Main-chain chiral poly(2-oxazoline)s: Influence of alkyl side-chain on secondary structure formation in solution

2011 ◽  
Vol 49 (13) ◽  
pp. 2790-2801 ◽  
Author(s):  
Meta M. Bloksma ◽  
Sarah Rogers ◽  
Ulrich S. Schubert ◽  
Richard Hoogenboom
Keyword(s):  
Secondary Structure ◽  
Structure Formation ◽  
Main Chain ◽  
Side Chain ◽  
Alkyl Side Chain ◽  
Secondary Structure Formation

scholarly journals ATP-induced asymmetric pre-protein folding: a driver of protein translocation?

2017 ◽  
Author(s):  
Robin A. Corey ◽  
William J. Allen ◽  
Ian Collinson
Keyword(s):  
Secondary Structure ◽  
Structure Formation ◽  
Protein Transport ◽  
Protein Translocation ◽  
Protein Secondary Structure ◽  
Structural Data ◽  
Underlying Mechanism ◽  
Dynamics Simulation ◽  
Secondary Structure Formation ◽  
Atp Binding And Hydrolysis

AbstractThe transport of proteins across membranes is a fundamental and essential process, achieved in every cell by the ‘Sec’ translocon. In prokaryotes, SecYEG associates with the motor protein SecA to carry out ATP-driven pre-protein secretion – a vital step in the biogenesis of most periplasmic, outer membrane and secreted proteins. Structural data of the SecA-SecYEG complex has provided considerable insight into underlying mechanism of this process. Previously, we have proposed a Brownian ratchet model for protein translocation, whereby the free energy of ATP binding and hydrolysis favours the progression of pre-protein across the membrane from the cytosol toward the outside [Allen, Corey et al. eLife 2016]. Here, we use atomistic molecular dynamics simulation of a SecA-SecYEG complex engaged with preprotein to further address the mechanism underlying this process. The data describe pre-protein secondary structure formation within the channel, which exhibits a nucleotide-dependent asymmetry between the cytoplasmic and exterior cavities. The results suggest ATP-dependent pre-protein transport is partly driven by pre-protein secondary structure formation. The model previously described, and refined here, could easily be adapted for the transport of proteins across various other membranes, such as the endoplasmic reticular and mitochondrial inner membranes.

Effects of Arginine Deimination and Citrulline Side‐Chain Length on Peptide Secondary Structure Formation

ChemBioChem ◽  
2019 ◽  
Vol 20 (16) ◽  
pp. 2118-2124
Author(s):  
Po‐Yi Wu ◽  
Chin‐Yi Chen ◽  
Jhe‐Hao Li ◽  
Jin‐Kai Lin ◽  
Ting‐Hsuan Chen ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Structure Formation ◽  
Chain Length ◽  
Side Chain ◽  
Side Chain Length ◽  
Secondary Structure Formation ◽  
Peptide Secondary Structure

scholarly journals Main-Chain Chiral Poly(2-oxazoline)s: Influence of Alkyl Side-Chain on Secondary Structure Formation in the Solid State

2015 ◽  
Vol 350 (1) ◽  
pp. 43-54 ◽  
Author(s):  
Meta M. Bloksma ◽  
Marco M. R. M. Hendrix ◽  
Silke Rathgeber ◽  
Ulrich S. Schubert ◽  
Richard Hoogenboom
Keyword(s):  
Solid State ◽  
Secondary Structure ◽  
Structure Formation ◽  
Main Chain ◽  
Side Chain ◽  
Alkyl Side Chain ◽  
Secondary Structure Formation
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