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Hire Dr. Rajaraman K.

United States

USD 150 /hr

Free lance biochemist and structural biologist

Profile Summary

Research scientist with PhD in Biochemistry and Biophysics and over 20 years of experience studying protein interactions, folding, aggregation and misfolding. Detailed knowledge of protein engineering and SAR-based drug design.

Subject Matter Expertise

• ☆ Biochemistry
• ☆ Biophysics
• ☆ Protein/Enzyme Engineering
• ☆ Alzheimer's Disease
• ☆ Severe Acute Respiratory Syndrome (SARS)

Services

• Writing
• Research
• Consulting
• Data & AI
• Product Development

Work Experience

Vice President Discovery Research

Proclara Biosciences

March 2018 - Present

Post Doctoral Associate

Whitehead Institute for Biomedical Research

October 2001 - May 2010

Education

PhD

Centre for Cellular and Molecular Biology CSIR

June 1995 - May 2001

Certifications

• Certification details not provided.

Publications

JOURNAL ARTICLE

(2019). Stability and Inter-domain Interactions Modulate Amyloid Binding Activity of a General Amyloid Interaction Motif . Journal of molecular biology.

(2017). Conformation as the Therapeutic Target for Neurodegenerative Diseases . Current Alzheimer research.

(2016). NPT088 reduces both amyloid-β and tau pathologies in transgenic mice . Alzheimer's & dementia (New York, N. Y.).

(2015). Remodeling Amyloid Fibers: Baker's Yeast Shows Us the Way . Chemistry & biology.

(2014). A bacteriophage capsid protein provides a general amyloid interaction motif (GAIM) that binds and remodels misfolded protein assemblies . Journal of molecular biology.

(2012). Conserved features of intermediates in amyloid assembly determine their benign or toxic states . Proceedings of the National Academy of Sciences of the United States of America.

(2011). Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins . Molecular cell.

(2011). The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication . The EMBO journal.

(2008). Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs . Proceedings of the National Academy of Sciences of the United States of America.

(2007). A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures . Proceedings of the National Academy of Sciences of the United States of America.

(2005). Structural insights into a yeast prion illuminate nucleation and strain diversity . Nature.

(2004). Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro . Proceedings of the National Academy of Sciences of the United States of America.

(2001). Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation . FEBS letters.

(1998). The chaperone-like alpha-crystallin forms a complex only with the aggregation-prone molten globule state of alpha-lactalbumin . Biochemical and biophysical research communications.

(1998). Structural perturbation of alpha-crystallin and its chaperone-like activity . International journal of biological macromolecules.

(1996). Molten-globule state of carbonic anhydrase binds to the chaperone-like alpha-crystallin . The Journal of biological chemistry.