Principal determinants leading to transition state formation of a protein-protein complex, orientation trumps side-chain interactions. - Wikidata - wikimedia - TriplyDB

Principal determinants leading to transition state formation of a protein-protein complex, orientation trumps side-chain interactions.

Principal determinants leading to transition state formation of a protein-protein complex, orientation trumps side-chain interactions.

http://www.wikidata.org/entity/Q37115153

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Two Independent Histidines, One in Human Prolactin and One in Its Receptor, Are Critical for pH-dependent Receptor Recognition and Activation A De Novo Protein Binding Pair By Computational Design and Directed Evolution Distinct ETA receptor binding mode of macitentan as determined by site directed mutagenesis Relationship between the architecture of zinc coordination and zinc binding affinity in proteins--insights into zinc regulation.Wrapping mimicking in drug-like small molecules disruptive of protein-protein interfaces.A biosensor study indicating that entropy, electrostatics, and receptor glycosylation drive the binding interaction between interleukin-7 and its receptor.

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Principal determinants leading to transition state formation of a protein-protein complex, orientation trumps side-chain interactions.

http://www.wikidata.org/entity/Q37115153

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 05 February 2009

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Principal determinants leading ...... rumps side-chain interactions.

@en

Principal determinants leading ...... rumps side-chain interactions.

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type

label

Principal determinants leading ...... rumps side-chain interactions.

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Principal determinants leading ...... rumps side-chain interactions.

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prefLabel

Principal determinants leading ...... rumps side-chain interactions.

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Principal determinants leading ...... rumps side-chain interactions.

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PNAS.0809800106

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Proceedings of the National Academy of Sciences of the United States of America

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Principal determinants leading ...... rumps side-chain interactions.

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Anthony A Kossiakoff

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James R Horn

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P2860

The X-ray structure of a growth hormone-prolactin receptor complex

Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity

Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil

The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding

A hot spot of binding energy in a hormone-receptor interface

Coupling of local folding to site-specific binding of proteins to DNA

High affinity RNase S-peptide variants obtained by phage display have a novel "hot-spot" of binding energy.

The functional binding epitope of a high affinity variant of human growth hormone mapped by shotgun alanine-scanning mutagenesis: insights into the mechanisms responsible for improved affinity.

Dissecting the binding energy epitope of a high-affinity variant of human growth hormone: cooperative and additive effects from combining mutations from independently selected phage display mutagenesis libraries.

Shotgun alanine scanning shows that growth hormone can bind productively to its receptor through a drastically minimized interface.

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2559-2564

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scholarly article

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10.1073/PNAS.0809800106

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8

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106

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Tobin R Sosnick

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2009-02-05T00:00:00Z

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23983317

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19196954

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2650303

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