Publications

Displaying 26 - 29 of 29

Phosphorylation-induced conformational dynamics in an intrinsically disordered protein and potential role in phenotypic heterogeneity

June 2, 2017

Author(s)

Prakash Kulkarni, Mohit Jolly, Dongya Jia, Steven Mooney, Ajay Bhargava, Luciane Kagohara, Yihong Chen, Pengyu Hao, Yanan He, Roberft Veltri, Alexander Grishaev, Keith Weninger, Herbert Levine, John Orban

Intrinsically disordered proteins (IDPs) that lack a unique 3D structure and comprise a large fraction of the human proteome play important roles in numerous cellular functions. Prostate- Associated Gene 4 (PAGE4) is an IDP that acts as a potentiator of

Quantitative Characterization of Configurational Space Sampled by HIV-1 Nucleocapsid Using Solution NMR, X-ray Scattering and Protein Engineering

June 3, 2016

Author(s)

Alexander V. Grishaev, Lalit Deshmukh, Charles Schwieters, G. Marius Clore

Nucleic-acid-related events in the HIV-1 replication cycle are mediated by nucleocapsid, a small protein comprising two zinc knuckles connected by a short flexible linker and flanked by disordered termini. Combining experimental NMR residual dipolar

Side Chain Conformational Distributions of a Small Protein Derived from Model-Free Analysis of a Large Set of Residual Dipolar Couplings

November 1, 2015

Author(s)

Fang Li, Alexander Grishaev, Jinfa Ying, Adriaan Bax

Accurate quantitative measurement of structural dispersion in proteins remains a prime challenge to both X-ray crystallography and NMR spectroscopy. An approach based on measurement of many residual dipolar couplings (RDCs) in differentially orienting

Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering

September 14, 2015

Author(s)

Alexander Grishaev, Vicenzo Venditti, Charles Schwieters, G. Marius Clore

Enzyme I (EI) is the first component in the bacterial phosphotransferase system, a signal transduction pathway in which phosphoryl transfer through a series of bimolecular protein-protein interactions is coupled to sugar transport across the membrane. EI

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