Testing a Model for Predicting Protein Stability
{'Code': '07020000', 'Directorate': {'Abbreviation': 'ENG', 'LongName': 'Directorate For Engineering'}, 'Division': {'Abbreviation': 'CBET', 'LongName': 'Div Of Chem, Bioeng, Env, & Transp Sys'}}
{'SignBlockName': 'Robert M. Wellek'}
This expedited award for novel research project deals with the effects          of single or multiple amino acid substitutions on the following                 properties of the proteins: (1) changes of enthalpy and specific heat           of unfolding; (2) thermal stability; (3) resistance to chemical                 denaturants.  These effects are correlated in terms of a transfer free          energy density model in order to determine whether rational patterns            emerge.  To apply this model, the protein amino acid composition must           be known and the protein must consist of a single reversibly unfolding          domain.  Most current efforts to explain and predict protein                    properties, such as stability, center on an extremely complex approach          based on the protein's amino acid.  In contrast, this approach applies          chemical engineering phase equilibrium methods to predict the                   thermodynamic parameters of protein stabilization.  This is a                   composition based approach, rather than a sequence approach; and it             goes directly counter to most current biochemical thinking on protein           property prediction.                                                                                                                                            One of the key questions in biotechnology processes is the stability            of the protein.  Until now, there have been no quantitative tools for           predicting protein stability.  If this model is successful, it will             provide a rational basis for site-directed mutagenesis to modify the            thermal stability (and hence the protease resistance and in vivo                turnover rates) of proteins.  Such a predictive tool would also permit          one to predict the temperature of maximum stability and thus to guide           protein processing and refolding operations.  This transfer free                energy density model is the first such quantitative tool.
{'FirstName': 'Bruce', 'LastName': 'Dale', 'EmailAddress': 'bdale@egr.msu.edu', 'StartDate': '08/15/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Colorado State University', 'CityName': 'Fort Collins', 'ZipCode': '805232002', 'PhoneNumber': '9704916355', 'StreetAddress': '601 S Howes St', 'CountryName': 'United States', 'StateName': 'Colorado', 'StateCode': 'CO'}
[{'Code': '1414', 'Text': 'INTERFAC PROCESSES & THERMODYN'}, {'Code': '1491', 'Text': 'Cellular & Biochem Engineering'}]
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8815543.xml'}