Literature DB >> 7632721

CD and NMR determination of the solution structure of a peptide corresponding to T4 lysozyme residues 38-51.

L V Najbar1, D J Craik, J D Wade, F Lin, M J McLeish.   

Abstract

Solid phase methods have been used to synthesise a peptide corresponding to residues 38-51 of T4 lysozyme. The peptide, LYS(38-51), encompasses helix B in the crystal structure of T4 lysozyme. CD and 1H-NMR analysis showed that the peptide was unstructured in aqueous solution but adopted a helical conformation in the more hydrophobic environment provided by 50% TFE and SDS micelles. The solution structure derived from the NMR data was similar to that of the helix in the X-ray structure, although there was some fraying at the N-terminus.

Entities:  

Mesh:

Substances:

Year:  1995        PMID: 7632721     DOI: 10.1016/0167-4838(95)00045-v

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Subdomain interactions as a determinant in the folding and stability of T4 lysozyme.

Authors:  M Llinás; S Marqusee
Journal:  Protein Sci       Date:  1998-01       Impact factor: 6.725

2.  Environmental polarity induces conformational transitions in a helical peptide sequence from bacteriophage T4 lysozyme and its tandem duplicate: a molecular dynamics simulation study.

Authors:  Harpreet Kaur; Yellamraju U Sasidhar
Journal:  J Mol Model       Date:  2015-03-17       Impact factor: 1.810

3.  Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding.

Authors:  M Sagermann; W A Baase; B W Matthews
Journal:  Proc Natl Acad Sci U S A       Date:  1999-05-25       Impact factor: 11.205

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.