Literature DB >> 11178002

Hydrogen bonds in polymer folding.

J Borg1, M H Jensen, K Sneppen, G Tiana.   

Abstract

We studied the thermodynamics of a homopolymeric chain with both van der Waals and directed hydrogen bond interaction. The effect of hydrogen bonds is to reduce dramatically the entropy of low-lying states and to give rise to long-range order and to conformations displaying secondary structures. For compact polymers a transition is found between helix-rich states and low-entropy sheet-dominated states. The consequences of this transition for protein folding and, in particular, for the problem of prions are discussed.

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Year:  2001        PMID: 11178002     DOI: 10.1103/PhysRevLett.86.1031

Source DB:  PubMed          Journal:  Phys Rev Lett        ISSN: 0031-9007            Impact factor:   9.161


  2 in total

1.  Importance of secondary structural specificity determinants in protein folding: insertion of a native beta-sheet sequence into an alpha-helical coiled-coil.

Authors:  Stanley C Kwok; Colin T Mant; Robert S Hodges
Journal:  Protein Sci       Date:  2002-06       Impact factor: 6.725

2.  A theoretical study of red-shifting and blue-shifting hydrogen bonds occurring between imidazolidine derivatives and PEG/PVP polymers.

Authors:  Boaz G Oliveira; Maria C A Lima; Ivan R Pitta; Suely L Galdino; Marcelo Z Hernandes
Journal:  J Mol Model       Date:  2009-06-12       Impact factor: 1.810

  2 in total

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