Genetic Studies of How Turns Affect Protein Stucture - Michael Hecht

Abstract

Funding Agency

Agency: National Institute of Health (NIH)
Institute: National Institute of General Medical Sciences (NIGMS)
Type: First Independent Research Support & Transition (FIRST) Awards (R29)
Project #: 5R29GM047877-05
Application #: 2185284
Study Section: Molecular and Cellular Biophysics Study Section (BBCA)

Project Start: 1992-08-01
Project End: 1997-07-31
Budget Start: 1996-08-01
Budget End: 1997-07-31
Support Year: 5
Fiscal Year: 1996
Total Cost
Indirect Cost

Institution

Name: Princeton University
Department: Chemistry
Type: Schools of Arts and Sciences
DUNS #: 002484665

City: Princeton
State: NJ
Country: United States
Zip Code: 08544

Related projects


NIH 1996 R29 GM	Genetic Studies of How Turns Affect Protein Stucture Hecht, Michael H. / Princeton University
NIH 1995 R29 GM	Genetic Studies of How Turns Affect Protein Stucture Hecht, Michael H. / Princeton University
NIH 1994 R29 GM	Genetic Studies of How Turns Affect Protein Stucture Hecht, Michael H. / Princeton University
NIH 1993 R29 GM	Genetic Studies of How Turns Affect Protein Stucture Hecht, Michael H. / Princeton University
NIH 1992 R29 GM	Genetic Studies of How Turns Affect Protein Stucture Hecht, Michael H. / Princeton University

Publications

Ybe, J A; Hecht, M H (1994) Periplasmic fractionation of Escherichia coli yields recombinant plastocyanin despite the absence of a signal sequence. Protein Expr Purif 5:317-23

Johnson, B H; Hecht, M H (1994) Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing. Biotechnology (N Y) 12:1357-60

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