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Ribonuclease T1: Structure, Function, and Stability
Author(s) -
Pace C. Nick,
Heinemann Udo,
Hahn Ulrich,
Saenger Wolfram
Publication year - 1991
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199103433
Subject(s) - protein folding , globular protein , folding (dsp implementation) , ribonuclease , sequence (biology) , protein structure , amino acid , nuclear magnetic resonance spectroscopy , peptide sequence , computational biology , chemistry , function (biology) , biophysics , biochemistry , biology , stereochemistry , rna , genetics , electrical engineering , gene , engineering
Proteins carry out the most important and difficult tasks in all living organisms. To do so, they must often interact specifically with other small and large molecules. This requires that they fold to a globular conformation with a unique active site that is used for the specific interaction. Consequently, protein folding can be regarded as the “secret of life”. Biochemists and chemists have a great interest in elucidating the mechanism by which proteins fold and in predicting the folded conformation and its stability given just the amino acid sequence. This challenge is sometimes called the “protein folding problem”. The ability to construct proteins differing in sequence by one or more amino acids and to analyze their three‐dimensional structures by X‐ray crystallography and NMR spectroscopy is a powerful tool for investigating the conformational stability and folding of proteins. Several proteins are now under intensive study by this approach. One of these is ribonuclease T1.