Resonance assignments of wild-type and two cysteine-free variants of the four-helix bundle protein, Rop.

Abstract:

:Repressor of primer (Rop, or ROM, RNA I modulator) is a 63 amino acid four-helix bundle protein that exists in solution as an anti-parallel homodimer. This protein has been extensively studied, including by X-ray crystallography, NMR, rational design, and combinatorial mutagenesis. Previous NMR experiments with wild-type Rop were carried out at pH 2.3 and pH 6.3. In this paper, we report complete N-H backbone assignments for three variants of Rop under the same pH 6.3 conditions: wild-type Rop; a cysteine-free pseudo-wild type variant (C38A C52V); and a core-repacked variant of the Cys-free variant (T19V L41V C38A C52V). These assignments enable functional and dynamic studies of wild-type and Cys-free variants of Rop.

journal_name

Biomol NMR Assign

authors

Bowles DP,Yuan C,Stephany KR,Lavinder JJ,Hansen AL,Magliery TJ

doi

10.1007/s12104-018-9837-0

subject

Has Abstract

pub_date

2018-10-01 00:00:00

pages

345-350

issue

2

eissn

1874-2718

issn

1874-270X

pii

10.1007/s12104-018-9837-0

journal_volume

12

pub_type

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