Publication Date:
1996-01-19
Description:
Small proteins or protein domains generally require disulfide bridges or metal sites for their stabilization. Here it is shown that the beta beta alpha architecture of zinc fingers can be reproduced in a 23-residue polypeptide in the absence of metal ions. The sequence was obtained through an iterative design process. A key feature of the final design is the incorporation of a type II' beta turn to aid in beta-hairpin formation. Nuclear magnetic resonance analysis reveals that the alpha helix and beta hairpin are held together by a defined hydrophobic core. The availability of this structural template has implications for the development of functional polypeptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Struthers, M D -- Cheng, R P -- Imperiali, B -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):342-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553067" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Circular Dichroism
;
DNA-Binding Proteins/chemistry
;
*Genes, Synthetic
;
Magnetic Resonance Spectroscopy
;
Models, Molecular
;
Molecular Sequence Data
;
Peptides/*chemistry
;
*Protein Engineering
;
Protein Folding
;
Protein Structure, Secondary
;
*Protein Structure, Tertiary
;
Proteins/*chemistry
;
Transcription Factors/chemistry
;
Zinc Fingers
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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