Principles that govern the folding of protein chains.

By C. Anfinsen. 1973

Subfields: Computational Biology & Bioinformatics

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Citations in the corpus

Modeling aspects of the language of life through transfer-learning protein sequences (2019, background): “Protein sequence largely determines protein structure, which somehow determines protein function [48].”
Critical Assessment of Methods of Protein Structure Prediction (CASP) – Progress and New directions in Round XI (2016, background): “Some examples: (1) For the complex of the protein kinase II leucine zipper and the ab11b GTPase (targets 797 and 798), the question of interest was the relative orientation of the components of the heterodimer.”
Diffusion probabilistic modeling of protein backbones in 3D for the motif-scaffolding problem (2022, neutral): “Anfinsen’s hypothesis states that the ground state conformation is thermodynamically accessible (Anfinsen, 1973), providing a mapping from sequence to a unique (ground state) structure.”
Ab Initio Protein Structure Assembly Using Continuous Structure Fragments and Optimized Knowledge-based Force Field (2012, background): “(1)–(13) to the TM-score, which are calculated from the average of 145 targets, each of which has 5000 structural decoys.”
Interconversion between two unrelated protein folds in the lymphotactin native state (2008, background): “Anfinsen’s hypothesis (1) continues to inform our basic understanding of protein folding: a polypeptide achieves its biologically active, native state by descending to the most thermodynamically stable configuration, which corresponds to one of a few thousand unique folds (2).”
Therapeutic approaches to protein-misfolding diseases (2003, background): “jpg" NDATA ITEM> ]> How and whether a protein folds in vivo are influenced primarily by its amino-acid sequence and the cellular environment surrounding the polypeptide chai”
Converging concepts of protein folding in vitro and in vivo (2009, background): “(1) Substrate protein may be delivered to GroEL by DnaK–DnaJ in a non-”
In and out of the ER: protein folding, quality control, degradation, and related human diseases. (2007, background): “Studies performed in test tubes in the early 1960s (6, 7, 407) revealed that only the information contained in the amino acid sequence is required for proper folding of polypeptides and that the unique native state of a protein in its physiologic milieu is the one in which the Gibbs free energy of t”