Literature DB >> 11119649

Quantitative comparison of the ability of hydropathy scales to recognize surface beta-strands in proteins.

C C Palliser1, D A Parry.   

Abstract

Methods based on the use of hydropathy scales have been used widely to ascertain the secondary structures of proteins. However, over 100 such scales have been reported in the literature, and which of these is the most successful in terms of the prediction rate of the correct structure is not clear. This article, therefore, reports a comprehensive analysis of the relative success of hydropathy scales to locate beta-strands on the surfaces of proteins. The technique we used is based on the technique proposed by Fraser and Parry, but it includes a modification that allows a higher rate of successful prediction and a lower rate of overprediction. We used as a basis for assessing the predictions a database of sequence-unique structures that we previously established. Proteins 2001;42:243-255. Copyright 2000 Wiley-Liss, Inc.

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Year:  2001        PMID: 11119649     DOI: 10.1002/1097-0134(20010201)42:2<243::aid-prot120>3.0.co;2-b

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  9 in total

1.  Determination of intrinsic hydrophilicity/hydrophobicity of amino acid side chains in peptides in the absence of nearest-neighbor or conformational effects.

Authors:  James M Kovacs; Colin T Mant; Robert S Hodges
Journal:  Biopolymers       Date:  2006       Impact factor: 2.505

Review 2.  Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: comparison with other hydrophilicity/hydrophobicity scales.

Authors:  Colin T Mant; James M Kovacs; Hyun-Min Kim; David D Pollock; Robert S Hodges
Journal:  Biopolymers       Date:  2009       Impact factor: 2.505

3.  Improved coarse-grained model for studying sequence dependent phase separation of disordered proteins.

Authors:  Roshan Mammen Regy; Jacob Thompson; Young C Kim; Jeetain Mittal
Journal:  Protein Sci       Date:  2021-05-24       Impact factor: 6.993

4.  A generalized analysis of hydrophobic and loop clusters within globular protein sequences.

Authors:  Richard Eudes; Khanh Le Tuan; Jean Delettré; Jean-Paul Mornon; Isabelle Callebaut
Journal:  BMC Struct Biol       Date:  2007-01-08

5.  A protein evolution model with independent sites that reproduces site-specific amino acid distributions from the Protein Data Bank.

Authors:  Ugo Bastolla; Markus Porto; H Eduardo Roman; Michele Vendruscolo
Journal:  BMC Evol Biol       Date:  2006-05-31       Impact factor: 3.260

6.  Wiggle-predicting functionally flexible regions from primary sequence.

Authors:  Jenny Gu; Michael Gribskov; Philip E Bourne
Journal:  PLoS Comput Biol       Date:  2006-06-05       Impact factor: 4.475

7.  Topological transformations in proteins: effects of heating and proximity of an interface.

Authors:  Yani Zhao; Mateusz Chwastyk; Marek Cieplak
Journal:  Sci Rep       Date:  2017-01-04       Impact factor: 4.379

8.  Repertoire-scale measures of antigen binding.

Authors:  Rohit Arora; Ramy Arnaout
Journal:  Proc Natl Acad Sci U S A       Date:  2022-08-15       Impact factor: 12.779

9.  Impact of residue accessible surface area on the prediction of protein secondary structures.

Authors:  Amir Momen-Roknabadi; Mehdi Sadeghi; Hamid Pezeshk; Sayed-Amir Marashi
Journal:  BMC Bioinformatics       Date:  2008-08-31       Impact factor: 3.169

  9 in total

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