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(1)H, (13)C and (15)N NMR backbone assignments of the 269-residue serine protease PB92 from Bacillus alcalophilus.

Abstract：

:The (1)H, (13)C and (15)N NMR resonances of the backbone of serine protease PB92 have been assigned. This 269-residue protein is one of the largest monomeric proteins assigned so far. The amount and quality of information available suggest that even larger proteins could be assigned with present methods. Measured chemical shifts show excellent agreement with the secondary structure.

journal_name

J Biomol NMR

journal_title

Journal of biomolecular NMR

authors

Fogh RH,Schipper D,Boelens R,Kaptein R

doi

10.1007/BF00178340

subject

Has Abstract

pub_date

1994-01-01 00:00:00

pages

123-8

issue

1

eissn

0925-2738

issn

1573-5001

journal_volume

4

pub_type

杂志文章

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