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Marta Manning remembers once when growing up in Hudson , N.Y. , she cut her finger, put it to her lips, “and it tasted like iron,” she said, making a connection between the bleeding cut and the mineral, yet wondering how they were related. That curiosity and drive to connect pieces of information have always led her to find new challenges, she said.

When she arrived at Rensselaer , Manning’s adviser recognized her driving curiosity. Sensing the potential for independent research, he assigned her a project studying protein mis-folding, a process thought to underlie several debilitating diseases, such as Alzheimer’s and type II diabetes. Eager to live up to the challenge, she began by focusing on stable proteins, which are unlikely to mis-fold. What makes them stable, she asked? And, can an unstable protein be redesigned with the characteristics of a stable one?

To find an answer, she helped develop a new technique — a way to identify stable proteins quickly — that has the potential to answer those questions. That breakthrough, she said, will help her continue looking for the answer as a graduate researcher at Rensselaer .

“Marta’s results are a methodological breakthrough that will potentially lead to a breakthrough in our understanding of kinetic stability in proteins,” said her adviser, Assistant Professor of Chemistry Wilfredo Colón. “Her work has been submitted to a first-rate scientific journal.”

Published in:

• Biochemistry

Articles and Abstracts:

"Structural Basis of Protein Kinetic Stability: Resistance to Sodium Dodecyl Sulfate Suggests a Central Role for Rigidity and a Bias Toward - β Sheet Structure" Marta Manning and Wilfredo Colón. Biochemistry, 43 (35), 11248 -11254, 2004. 10.1021/bi0491898 S0006-2960(04)09189-5

Department of Chemistry and Chemical Biology