Literature DB >> 16008490

Proteins and polymers.

Jayanth R Banavar1, Trinh Xuan Hoang, Amos Maritan.   

Abstract

Proteins, chain molecules of amino acids, behave in ways which are similar to each other yet quite distinct from standard compact polymers. We demonstrate that the Flory theorem, derived for polymer melts, holds for compact protein native state structures and is not incompatible with the existence of structured building blocks such as alpha helices and beta strands. We present a discussion on how the notion of the thickness of a polymer chain, besides being useful in describing a chain molecule in the continuum limit, plays a vital role in interpolating between conventional polymer physics and the phase of matter associated with protein structures.

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Year:  2005        PMID: 16008490     DOI: 10.1063/1.1940059

Source DB:  PubMed          Journal:  J Chem Phys        ISSN: 0021-9606            Impact factor:   3.488


  5 in total

1.  Does amino acid sequence determine the properties of Aβ dimer?

Authors:  Christopher Lockhart; Seongwon Kim; Rashmi Kumar; Dmitri K Klimov
Journal:  J Chem Phys       Date:  2011-07-21       Impact factor: 3.488

2.  Statistics of knots, geometry of conformations, and evolution of proteins.

Authors:  Rhonald C Lua; Alexander Y Grosberg
Journal:  PLoS Comput Biol       Date:  2006-05-19       Impact factor: 4.475

3.  Mechanical Unfolding of Single Polyubiquitin Molecules Reveals Evidence of Dynamic Disorder.

Authors:  Prasanta Kundu; Soma Saha; Gautam Gangopadhyay
Journal:  ACS Omega       Date:  2020-04-15

4.  Statistical potentials from the Gaussian scaling behaviour of chain fragments buried within protein globules.

Authors:  Stefano Zamuner; Flavio Seno; Antonio Trovato
Journal:  PLoS One       Date:  2022-01-27       Impact factor: 3.240

5.  Polymer uncrossing and knotting in protein folding, and their role in minimal folding pathways.

Authors:  Ali R Mohazab; Steven S Plotkin
Journal:  PLoS One       Date:  2013-01-24       Impact factor: 3.240

  5 in total

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