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PMID: 6401108 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

Solution NMR studies of intact lambda repressor.

Journal of biomolecular structure & dynamics ·Vol. 1 ·No. 1 ·1983-10-00 ·Pages 151-7

Weiss MA, Karplus M, Patel DJ, Sauer RT

Abstract

Using a combination of two and one-dimensional NMR spectroscopy, it is shown that in the intact bacteriophage lambda repressor, the N-terminal domain assumes the same global structure as when it remains isolated. It is further shown that the N-terminal domain is only loosely attached to the C-terminal domain in the intact repressor.

MeSH Terms

DNA-Binding Proteins Magnetic Resonance Spectroscopy Molecular Structure Repressor Proteins Solutions Transcription Factors Viral Proteins Viral Regulatory and Accessory Proteins

Chemicals

DNA-Binding Proteins Repressor Proteins Solutions Transcription Factors Viral Proteins Viral Regulatory and Accessory Proteins phage repressor proteins

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Weiss M A

Department of Chemistry, Harvard University, Cambridge MA 02138.

Karplus M

Patel D J

Sauer R T

Article Info

Journal

Journal of biomolecular structure & dynamics

Abbr.

J Biomol Struct Dyn

ISSN

0739-1102

DOI

10.1080/07391102.1983.10507431

Published

1983-10-00

Pages

151-7

Language

English

Region

England

NLM ID

8404176

Subset

Grants

NIAID NIH HHS · AI-15706 · United States

NCRR NIH HHS · RR-00995 · United States

External Links

PubMed source DOI: 10.1080/07391102.1983.10507431 View journal details

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Solution NMR studies of intact lambda repressor.

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