Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion
- 4 April 1997
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 267 (3), 749-761
- https://doi.org/10.1006/jmbi.1997.0904
Abstract
No abstract availableKeywords
This publication has 58 references indexed in Scilit:
- The PROSITE dictionary of sites and patterns in proteins, its current statusNucleic Acids Research, 1993
- Purification and sequencing of cytochrome b from potato reveals methionine cleavage of a mitochondriallly encoded proteinFEBS Letters, 1993
- A Method to Identify Protein Sequences That Fold into a Known Three-Dimensional StructureScience, 1991
- Deciphering the Message in Protein Sequences: Tolerance to Amino Acid SubstitutionsScience, 1990
- Identification of protein folds: Matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structuresProteins-Structure Function and Bioinformatics, 1990
- Identifying determinants of folding and activity for a protein of unknown structure.Proceedings of the National Academy of Sciences of the United States of America, 1989
- Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coliGene, 1988
- Endogenous synthesis of formyl-methionine peptides in isolated mitochondria and chloroplastsBiochemical and Biophysical Research Communications, 1971
- On the release of the formyl group from nascent proteinJournal of Molecular Biology, 1968
- N-formylmethionyl-sRNA as the initiator of protein synthesis.Proceedings of the National Academy of Sciences of the United States of America, 1966