Author

R. Kudva

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Assay:proteomics· 3 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Organism:E. coli· 1 Approach:microscopy & imaging analysis· 1 Organism:plant (other)· 1

Frequent Co-Authors

G. von Heijne· 4 shared P. Tian· 3 shared R. B. Best· 2 shared A. A. Nickson· 1 shared A. Andersson· 1 shared A. Katranidis· 1 shared A. Magoulopoulou· 1 shared A. Steward· 1 shared

Activity by Year

2018-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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4 shared papersBiophysics

G. von Heijne

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4 papers

Recent·Most cited

The ribosome modulates folding inside the ribosomal exit tunnel

F. Wruck, P. Tian, R. Kudva, R. B. Best, G. von Heijne, S. J. Tans, A. Katranidis

The paper investigates how the ribosomal exit tunnel affects the folding of a small zinc-finger domain, finding that electrostatic interactions, not just confinement, contribute to folding acceleration and stabilization.

bioRxiv · Jun 30, 2020Biophysics

Membrane integration and topology of RIFIN and STEVOR proteins of the Plasmodium falciparum parasite

A. Andersson, R. Kudva, A. Magoulopoulou, Q. Lejarre, P. Lara, P. Xu, S. Goel, J. Pissi, X. Ru, T. Hessa, M. Wahlgren, G. Von Heijne, I. Nilsson, A. Tellgren-Roth

The paper investigates the membrane topology of RIFIN and STEVOR proteins in Plasmodium falciparum using N-linked glycosylation to determine their ER membrane insertion patterns.

bioRxiv · May 29, 2019Biochemistry

The Shape of the Ribosome Exit Tunnel Affects Cotranslational Protein Folding

R. Kudva, P. Tian, F. Pardo-Avila, M. Carroni, R. B. Best, H. D. Bernstein, G. Von Heijne

The study shows that the geometry of the E. coli ribosome exit tunnel influences where proteins fold during translation, with larger domains folding deeper when tunnel space is available.

bioRxiv · Sep 25, 2018Biochemistry

The Folding Pathway of an Ig Domain is Conserved On and Off the Ribosome

P. Tian, A. Steward, R. Kudva, T. Su, P. J. Shilling, A. A. Nickson, J. J. Hollins, R. Beckmann, G. Von Heijne, J. Clarke, R. Best

The paper shows that the folding pathway of the titin I27 domain is conserved whether folding occurs on or off the ribosome.

bioRxiv · Jun 18, 2018Biophysics