How a highly acidic SH3 domain folds in the absence of its charged peptide target.

Autor: Jaramillo-Martinez V; Texas Tech University Health Sciences Center, Lubbock, Texas, 79430, USA.; Eastern New Mexico University, Portales, New Mexico, USA., Dominguez MJ; Texas Tech University Health Sciences Center, Lubbock, Texas, 79430, USA.; Eastern New Mexico University, Portales, New Mexico, USA., Bell GM; Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK., Souness ME; Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK., Carhart AH; Department of Chemistry, Skidmore College, Saratoga Springs, New York, 12866, USA., Cuibus MA; Department of Chemistry, Skidmore College, Saratoga Springs, New York, 12866, USA., Masoumzadeh E; Texas Tech University Health Sciences Center, Lubbock, Texas, 79430, USA., Lantz BJ; Eastern New Mexico University, Portales, New Mexico, USA., Adkins AJ; Department of Chemistry, Skidmore College, Saratoga Springs, New York, 12866, USA., Latham MP; Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA.; Department of Chemistry & Biochemistry, Texas Tech University, Lubbock, Texas, 79409, USA., Ball KA; Department of Chemistry, Skidmore College, Saratoga Springs, New York, 12866, USA., Stollar EJ; Eastern New Mexico University, Portales, New Mexico, USA.; Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.

Publikováno v: Protein science : a publication of the Protein Society [Protein Sci] 2023 May; Vol. 32 (5), pp. e4635.