
Matt HeberlingPeptone - The Protein Intelligence Company
Matt Heberling
PhD
About
12
Publications
2,380
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239
Citations
Citations since 2017
Introduction
Teaching AI machines protein physics for antibody optimization.
Additional affiliations
Education
October 2009 - June 2015
September 2007 - August 2009
September 2004 - June 2007
Publications
Publications (12)
Ammonia lyases (AL) and aminomutases (AM) are emerging in green synthetic routes to chiral amines and an AL is being explored as an enzyme therapeutic for treating phenylketonuria and cancer. Although the restricted substrate range of the wild-type enzymes limits their widespread application, the non-reliance on external cofactors and direct functi...
Deciphering the structural features that functionally separate ammonia lyases from aminomutases is of interest because it may allow for the engineering of more efficient aminomutases for the synthesis of unnatural amino acids (e.g., β-amino acids). However, this has proved to be a major challenge that involves understanding the factors that influen...
An overwhelming amount of experimental evidence suggests that elucidations of protein function, interactions, and pathology are incomplete without inclusion of intrinsic protein disorder and structural dynamics. Thus, to expand our understanding of intrinsic protein disorder, we have created a database of secondary structure (SS) propensities for p...
Pseudomonas species strain SBV1 can rapidly grow on medium containing β-valine as a sole nitrogen source. The tertiary amine feature of β-valine prevents direct deamination reactions catalyzed by aminotransferases, amino acid dehydrogenases, and amino acid oxidases. However, lyase- or aminomutase-mediated conversions would be possible. To identify...
##Assembly-Data-START## Sequencing Technology :: Sanger dideoxy sequencing ##Assembly-Data-END##
##Assembly-Data-START## Assembly Method :: CLC Genomics Workbench v. 4 Sequencing Technology :: Sanger dideoxy sequencing; Illumina ##Assembly-Data-END##
An aminomutase, naturally catalyzing the interconversion of (S)-α-phenylalanine and (R)-β-phenylalanine, was converted into an ammonia lyase catalyzing the nonoxidative deamination of phenylalanine to cinnamic acid by a rational single-point mutation. It could be shown by crystal structures and kinetic data that the flexibility of the lid that cove...
Turn to switch: A mutant of phenylalanine aminomutase was engineered that can catalyze the regioselective amination of cinnamate derivatives (see scheme, red) to, for example, β-amino acids. This regioselectivity, along with the X-ray crystal structures, suggests two distinct carboxylate binding modes differentiated by C(β)-C(ipso) bond rotation, w...
Aminomutases carry out the chemically challenging exchange of a hydrogen atom and an amine substituent present on neighboring carbon atoms. In recent years, aminomutases have been intensively investigated for their biophysical, structural and mechanistic characteristics. The reactions catalyzed by these enzymes have considerable potential for biote...
Projects
Projects (2)
Designed ankyrin repeat protein (DARPin) libraries consist of a consensus framework with a randomized binding surface. We use high-throughput ribosome display to select binders from these libraries. I design novel molecules which combine DARPins binding modules with other domains to generate new molecules tailor-made for specific functions: e.g. viral retargeting, interference with receptor signalling, crystallization chaperones.
See http://www.bioc.uzh.ch/plueckthun/index.php?pid=3-2-13 for a full list of publications out of the Plückthun Lab on this topic
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