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Updated: Jun 20, 2026

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

ペプチドの折り畳みを制御し,リン酸化アミノ酸とトリプトファンの間の排斥的な相互作用を行う

Alexander J Riemen1, Marcey L Waters

  • 1Department of Chemistry, CB 3290, University of North Carolina, Chapel Hill, North Carolina 27599, USA.

Journal of the American Chemical Society
|September 12, 2009
PubMed
まとめ

セリン,スレオニン,チロシンなどのアミノ酸のリン酸化は,排斥的な相互作用により,ベータヘアピン構造を1.0kcal/molで不安定化させます. この研究では,リン酸化がタンパク質の機能に影響を与える新しい方法が明らかになりました.

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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

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Protein Folding01:25

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Protein Folding01:22

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Protein Folding01:22

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
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Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...