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Your search keyword '"Schertler GFX"' showing total 3 results
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3 results on '"Schertler GFX"'

1. Photocrosslinking between nucleic acids and proteins: general discussion.

Author

Bhat V, Cogdell R, Crespo-Hernández CE, Datta A, De A, Haacke S, Helliwell J, Improta R, Joseph J, Karsili T, Kohler B, Krishnan R, L M, Lewis F, Mandal I, Markovitsi D, Mishra PP, Paul S, Periyasamy G, Pradeepkumar PI, Roy Chowdhury P, Sarangi M, Sasikumar D, Schapiro I, Schertler GFX, Schlichting I, Segarra-Martí J, Swaminathan R, V V, van Grondelle R, Varghese R, and Venkatramani R

Subjects
Photochemical Processes, Cross-Linking Reagents chemistry, DNA chemistry, Proteins chemistry
Published
2018
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2. Light induced charge and energy transport in nucleic acids and proteins: general discussion.

Author

Chattopadhyay A, Cogdell R, Crespo-Hernández CE, Datta A, De A, Haacke S, Hariharan M, Helliwell J, Hughes A, Improta R, Jones M, Joseph J, Karsili T, Kohler B, Krishnan R, Kuriakose A, L M, Markovitsi D, Medhi H, Periyasamy G, Pradeepkumar PI, Roy Chowdhury P, Sarangi M, Schapiro I, Schertler GFX, Schlichting I, Segarra-Martí J, Swaminathan R, V V, van Grondelle R, Venkatraman RK, Venkatramani R, and Watts A

Subjects
DNA chemistry, DNA radiation effects, Energy Transfer radiation effects, Light, Proteins chemistry, Proteins radiation effects
Published
2018
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3. Probing Gαi1 protein activation at single-amino acid resolution.

Author

Sun D, Flock T, Deupi X, Maeda S, Matkovic M, Mendieta S, Mayer D, Dawson R, Schertler GFX, Madan Babu M, and Veprintsev DB

Subjects
Amino Acids genetics, DNA Mutational Analysis, GTP-Binding Protein alpha Subunits chemistry, GTP-Binding Protein alpha Subunits genetics, Humans, Models, Molecular, Protein Binding, Protein Conformation, Protein Stability, Amino Acids metabolism, DNA metabolism, GTP-Binding Protein alpha Subunits metabolism, Rhodopsin metabolism
Abstract

We present comprehensive maps at single-amino acid resolution of the residues stabilizing the human Gαi1 subunit in nucleotide- and receptor-bound states. We generated these maps by measuring the effects of alanine mutations on the stability of Gαi1 and the rhodopsin-Gαi1 complex. We identified stabilization clusters in the GTPase and helical domains responsible for structural integrity and the conformational changes associated with activation. In activation cluster I, helices α1 and α5 pack against strands β1-β3 to stabilize the nucleotide-bound states. In the receptor-bound state, these interactions are replaced by interactions between α5 and strands β4-β6. Key residues in this cluster are Y320, which is crucial for the stabilization of the receptor-bound state, and F336, which stabilizes nucleotide-bound states. Destabilization of helix α1, caused by rearrangement of this activation cluster, leads to the weakening of the interdomain interface and release of GDP.

Published
2015
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