Work

The conformation of apamin

Year: 1986

Type: article

Abstract: Energy minimization techniques are used as a tool to distinguish between different proposed models for the structure of the bee venom polypeptide apamin. The influence of electrostatic interactions on the resultant energies is noted. The model of Hider and Ragnarsson [(1980) FEBS Lett. 111, 189-193] is found to be of consistently low energy.

Source: FEBS Letters

DOI: 10.1016/0014-5793(86)80344-1

Authors: C.M. Freeman, C.R.A. Catlow, A.M. Hemmings, R.C. Hider

Institutions: Keele University, Birkbeck, University of London, University of Essex

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W2011556019

FWCI: 0.838

Cites: 18

Cited by: 27

Related to: 10