Amide proton exchange in the alpha-amylase polypeptide inhibitor Tendamistat studied by two-dimensional 1H nuclear magnetic resonance.

Abstract:

:The individual amide proton exchange rates in Tendamistat at pH 3.0 and 50 degrees C were measured by using two-dimensional 1H nuclear magnetic resonance. Overall, it was found that the distribution of exchange rates along the sequence is dominated by the interstrand hydrogen bonds of the beta-sheet structures. The slowly exchanging protons in the core of the two beta-sheets were shown to exchange via an EX2 mechanism. Further analysis of the data indicates that different large-scale structure fluctuations are responsible for the exchange from the two beta-sheets, even though the three-dimensional structure of Tendamistat appears to consist of a single structural domain.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Wang QW,Kline AD,Wüthrich K

doi

10.1021/bi00394a030

subject

Has Abstract

pub_date

1987-10-06 00:00:00

pages

6488-93

issue

20

eissn

0006-2960

issn

1520-4995

journal_volume

26

pub_type

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