English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  How good are predictions of protein secondary structure?

Kabsch, W., & Sander, C. (1983). How good are predictions of protein secondary structure? FEBS Letters, 155(2), 179-182. doi:10.1016/0014-5793(82)80597-8.

Item is

Files

show Files
hide Files
:
FEBSLett_155_1983_179.pdf (Any fulltext), 340KB
 
File Permalink:
-
Name:
FEBSLett_155_1983_179.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Kabsch, Wolfgang1, 2, Author           
Sander, Christian, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: Protein structure; Secondary structure prediction; Amino acid sequence
 Abstract: The three most widely used methods for the prediction of protein secondary structure from the amino acid sequence are tested on 62 proteins of known structure using a program package and data collection not previously available. None of these methods predicts better than 56% of the residues correctly, for a three state model (helix, sheet and loop). The algorithms of Robson [J. Mol. Biol. (1978) 120, 97–120] and Lim [J. Mol. Biol. (1974) 88, 873–894] are the best of those tested. New methods, now under development, can be tested against this benchmark.

Details

show
hide
Language(s): eng - English
 Dates: 1983-02-172001-11-141983-05-08
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0014-5793(82)80597-8
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 155 (2) Sequence Number: - Start / End Page: 179 - 182 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501