Narasimha Sreerama

7.6k total citations · 4 hit papers
32 papers, 6.6k citations indexed

About

Narasimha Sreerama is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Narasimha Sreerama has authored 32 papers receiving a total of 6.6k indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 18 papers in Spectroscopy and 11 papers in Materials Chemistry. Recurrent topics in Narasimha Sreerama's work include Protein Structure and Dynamics (18 papers), Molecular spectroscopy and chirality (11 papers) and Enzyme Structure and Function (10 papers). Narasimha Sreerama is often cited by papers focused on Protein Structure and Dynamics (18 papers), Molecular spectroscopy and chirality (11 papers) and Enzyme Structure and Function (10 papers). Narasimha Sreerama collaborates with scholars based in United States, India and Germany. Narasimha Sreerama's co-authors include Robert W. Woody, R. W. Woody, S.Yu. Venyaminov, G. Blauer, Michael E. Powers, Mark C. Manning, David P. Goldenberg, Saraswathi Vishveshwara, Patrik R. Callis and Koji Nakanishi and has published in prestigious journals such as Journal of the American Chemical Society, The Journal of Chemical Physics and Journal of Molecular Biology.

In The Last Decade

Narasimha Sreerama

31 papers receiving 6.5k citations

Hit Papers

Estimation of Protein Secondary Structure from Circular D... 1993 2026 2004 2015 2000 1993 1999 2000 500 1000 1.5k 2.0k 2.5k
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set
    2000 2.6k citations Narasimha Sreerama, Robert W. Woody Analytical Biochemistry profile →
  2. A Self-Consistent Method for the Analysis of Protein Secondary Structure from Circular Dichroism
    1993 943 citations Narasimha Sreerama, R. W. Woody Analytical Biochemistry profile →
  3. Estimation of the number of α‐helical and β‐strand segments in proteins using circular dichroism spectroscopy
    1999 627 citations Narasimha Sreerama, S.Yu. Venyaminov et al. Protein Science profile →
  4. Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Inclusion of Denatured Proteins with Native Proteins in the Analysis
    2000 509 citations Narasimha Sreerama, S.Yu. Venyaminov et al. Analytical Biochemistry profile →

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Narasimha Sreerama United States 20 4.8k 1.0k 689 508 500 32 6.6k
Gerald R. Grimsley United States 24 5.5k 1.1× 1.6k 1.6× 550 0.8× 542 1.1× 592 1.2× 31 7.3k
Lee Whitmore United Kingdom 13 3.5k 0.7× 638 0.6× 363 0.5× 372 0.7× 344 0.7× 21 5.3k
Francesc Avilés Spain 52 7.1k 1.5× 1.3k 1.3× 455 0.7× 668 1.3× 903 1.8× 266 9.9k
Taiji Imoto Japan 39 4.1k 0.9× 1.5k 1.5× 561 0.8× 305 0.6× 355 0.7× 238 6.0k
Charles M. Deber Canada 55 7.5k 1.6× 478 0.5× 1.1k 1.6× 669 1.3× 633 1.3× 218 9.7k
Rainer Rudolph Germany 51 7.3k 1.5× 2.0k 2.0× 409 0.6× 635 1.3× 1.1k 2.2× 165 9.6k
Shohei Koide United States 52 7.0k 1.5× 955 0.9× 571 0.8× 530 1.0× 532 1.1× 169 9.7k
Frank Wien France 26 3.1k 0.6× 768 0.8× 426 0.6× 494 1.0× 258 0.5× 112 4.9k
Jean‐Marie Ruysschaert Belgium 41 4.4k 0.9× 414 0.4× 375 0.5× 473 0.9× 329 0.7× 110 6.7k
John M. Tomich United States 44 3.6k 0.8× 292 0.3× 375 0.5× 489 1.0× 360 0.7× 151 5.5k

Countries citing papers authored by Narasimha Sreerama

Since Specialization
Citations

This map shows the geographic impact of Narasimha Sreerama's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Narasimha Sreerama with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Narasimha Sreerama more than expected).

Fields of papers citing papers by Narasimha Sreerama

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Narasimha Sreerama. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Narasimha Sreerama. The network helps show where Narasimha Sreerama may publish in the future.

Co-authorship network of co-authors of Narasimha Sreerama

This figure shows the co-authorship network connecting the top 25 collaborators of Narasimha Sreerama. A scholar is included among the top collaborators of Narasimha Sreerama based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Narasimha Sreerama. Narasimha Sreerama is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Sreerama, Narasimha & Robert W. Woody. (2004). Computation and Analysis of Protein Circular Dichroism Spectra. Methods in enzymology on CD-ROM/Methods in enzymology. 383. 318–351. 428 indexed citations
2.
Sreerama, Narasimha & Robert W. Woody. (2003). Structural composition of βI‐ and βII‐proteins. Protein Science. 12(2). 384–388. 157 indexed citations
3.
Sreerama, Narasimha & Robert W. Woody. (2003). On the analysis of membrane protein circular dichroism spectra. Protein Science. 13(1). 100–112. 191 indexed citations
4.
Mou, Tung‐Chung, Narasimha Sreerama, Thomas C. Terwilliger, Robert W. Woody, & Donald M. Gray. (2002). Independent tyrosyl contributions to the CD of Ff gene 5 protein and the distinctive effects of Y41H and Y41F mutants on protein–protein cooperative interactions. Protein Science. 11(3). 601–613. 3 indexed citations
5.
Sreerama, Narasimha, S.Yu. Venyaminov, & Robert W. Woody. (2001). Analysis of Protein Circular Dichroism Spectra Based on the Tertiary Structure Classification. Analytical Biochemistry. 299(2). 271–274. 77 indexed citations
6.
Sreerama, Narasimha & Robert W. Woody. (2000). Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set. Analytical Biochemistry. 287(2). 252–260. 2574 indexed citations breakdown →
7.
Sreerama, Narasimha, S.Yu. Venyaminov, & Robert W. Woody. (2000). Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Inclusion of Denatured Proteins with Native Proteins in the Analysis. Analytical Biochemistry. 287(2). 243–251. 509 indexed citations breakdown →
8.
Sreerama, Narasimha & Robert W. Woody. (1999). Molecular dynamics simulations of polypeptide conformations in water: A comparison of α, β, and poly(pro)II conformations. Proteins Structure Function and Bioinformatics. 36(4). 400–406. 3 indexed citations
9.
Woody, Robert W. & Narasimha Sreerama. (1999). Comment on “Improving protein circular dichroism calculations in the far-ultraviolet through reparametrizing the amide chromophore” [J. Chem. Phys. 109, 782 (1998)]. The Journal of Chemical Physics. 111(6). 2844–2845. 64 indexed citations
10.
11.
Sreerama, Narasimha, S.Yu. Venyaminov, & Robert W. Woody. (1999). Estimation of the number of α‐helical and β‐strand segments in proteins using circular dichroism spectroscopy. Protein Science. 8(2). 370–380. 627 indexed citations breakdown →
12.
MEYERS, A. I., et al.. (1997). Synthesis and chiroptical properties of a novel C2-symmetric binaphthyl phosphortriamide (?chiral HMPA?). Chirality. 9(5-6). 431–434. 6 indexed citations
13.
Sreerama, Narasimha, et al.. (1994). Bacteriophage T7 RNA Polymerase and Its Active-site Mutants. Journal of Molecular Biology. 237(1). 5–19. 33 indexed citations
14.
Sreerama, Narasimha & Robert W. Woody. (1994). Poly(Pro)II Helixes in Globular Proteins: Identification and Circular Dichroic Analysis. Biochemistry. 33(33). 10022–10025. 221 indexed citations
15.
Sreerama, Narasimha & Robert W. Woody. (1994). Protein Secondary Structure from Circular Dichroism Spectroscopy. Journal of Molecular Biology. 242(4). 497–507. 168 indexed citations
16.
Sreerama, Narasimha & R. W. Woody. (1993). A Self-Consistent Method for the Analysis of Protein Secondary Structure from Circular Dichroism. Analytical Biochemistry. 209(1). 32–44. 943 indexed citations breakdown →
17.
Blauer, G., Narasimha Sreerama, & R. W. Woody. (1993). Optical activity of hemoproteins in the Soret region. Circular dichroism of the heme undecapeptide of cytochrome c in aqueous solution. Biochemistry. 32(26). 6674–6679. 110 indexed citations
18.
Sankararamakrishnan, Ramasubbu, Narasimha Sreerama, & Saraswathi Vishveshwara. (1991). Characterization of proline-containing right-handed α-helix by molecular dynamics studies. Biophysical Chemistry. 40(1). 97–108. 10 indexed citations
19.
Sreerama, Narasimha & Saraswathi Vishveshwara. (1989). Ab initio studies on proton transfer involving Schiff base and related nitrogen compounds. Journal of Molecular Structure. 212. 53–60. 3 indexed citations
20.
Sreerama, Narasimha & S. Vishveshwara. (1985). Studies involving the electrostatic potential of valinomycin. Journal of Biosciences. 8(1-2). 315–327. 1 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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