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Open AccessJournal ArticleDOI

Prediction of beta-turns

P.Y. Chou, +1 more
- 01 Jun 1979 - 
- Vol. 26, Iss: 3, pp 367-383
TLDR
Kohonen's self-organization model, a neural network model, is applied to predict the beta-turns in proteins, implying that the residue-coupled effect along a polypeptide chain is important for the formation of reversal turns during the process of protein folding.
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This article is published in Biophysical Journal.The article was published on 1979-06-01 and is currently open access. It has received 354 citations till now.

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Book ChapterDOI

Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins.

TL;DR: The aim of this chapter is to present recent developments in the vibrational spectroscopy of peptides, polypeptides, and proteins.
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Prediction of chain flexibility in proteins

TL;DR: This work has analyzed 31 refined protein structures to develop a method for predicting flexible segments from a given amino acid sequence and found that segmental flexibility is more indicative of an antigenic determinant than the selection criteria mentioned above.
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Bacteriophage lysis: mechanism and regulation.

TL;DR: The available evidence suggests that holins oligomerize to form nonspecific holes and that this hole-forming step is the regulated step in phage lysis, which is as much an essential feature of holin function as is the hole formation itself.
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SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane.

TL;DR: It is proposed that the function of the complex purified as a complex with two nonphosphorylated membrane glycoproteins is to regulate Ca(2+)-dependent retention mechanisms for luminal proteins of the endoplasmic reticulum.
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Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum.

TL;DR: A cDNA clone encoding the high affinity Ca2+-binding protein (HACBP) of rabbit skeletal muscle sarcoplasmic reticulum was isolated and sequenced, and the name calreticulin was chosen for the protein.
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