Backbone dynamics of cyclotide MCoTI-I free and complexed with trypsin

Shadakshara S. Puttamadappa; Krishnappa Jagadish; Alexander Shekhtman; Julio A. Camarero

doi:10.1002/anie.201002906

Backbone dynamics of cyclotide MCoTI-I free and complexed with trypsin

Shadakshara S. Puttamadappa
, Krishnappa Jagadish
, Alexander Shekhtman
, Julio A. Camarero

Chemistry

University at Albany

SUNY Albany
University of Southern California

Research output: Contribution to journal › Article › peer-review

50 Scopus citations

Abstract

Showing some backbone: Most of the backbone NH groups of cyclotide MCoTI-I are constrained in the free state, which results in a well-folded compact structure, as indicated by {15N,1H} NMR spectroscopy (see picture). According to the backbone order parameter S2, the backbone mobility in trypsin-bound MCoTI-I is significantly increased.

Original language	English
Pages (from-to)	7030-7034
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	49
Issue number	39
DOIs	https://doi.org/10.1002/anie.201002906
State	Published - Sep 17 2010

Keywords

Cyclotides
Moleculardynamics
NMR spectroscopy
Protein-protein interactions
Structural biology

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10.1002/anie.201002906

Cite this

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abstract = "Showing some backbone: Most of the backbone NH groups of cyclotide MCoTI-I are constrained in the free state, which results in a well-folded compact structure, as indicated by \{15N,1H\} NMR spectroscopy (see picture). According to the backbone order parameter S2, the backbone mobility in trypsin-bound MCoTI-I is significantly increased.",

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AU - Shekhtman, Alexander

AU - Camarero, Julio A.

PY - 2010/9/17

Y1 - 2010/9/17

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KW - Cyclotides

KW - Moleculardynamics

KW - NMR spectroscopy

KW - Protein-protein interactions

KW - Structural biology

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Backbone dynamics of cyclotide MCoTI-I free and complexed with trypsin

Abstract

Keywords

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