Relevant bibliographies by topics / Ramachandran Map

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters

Academic literature on the topic 'Ramachandran Map'

Author: Grafiati
Published: 4 June 2021
Last updated: 26 July 2025

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Journal articles on the topic "Ramachandran Map"

1

Ramakrishnan, C. "Ramachandran and his Map." Resonance 6, no. 10 (2001): 48–56. http://dx.doi.org/10.1007/bf02836967.

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2

Walther, Dirk, and Fred E. Cohen. "Conformational attractors on the Ramachandran map." Acta Crystallographica Section D Biological Crystallography 55, no. 2 (1999): 506–17. http://dx.doi.org/10.1107/s0907444998013353.

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Frequency distributions of protein backbone dihedral angles φ and ψ have been analyzed systematically for their apparent correlation with various crystallographic parameters, including the resolution at which the protein structures had been determined, the R factor and the free R factor, and the results have been displayed in novel differential Ramachandran maps. With improved sensitivity compared with conventionally derived heuristic Ramachandran maps, such differential maps automatically reveal conformational `attractors' to which φ/ψ distributions converge as the crystallographic resolution
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3

SZABADKA, ZOLTÁN, RAFAEL ÖRDÖG, and VINCE GROLMUSZ. "THE RAMACHANDRAN MAP OF MORE THAN 6,500 PERFECT POLYPEPTIDE CHAINS." Biophysical Reviews and Letters 02, no. 03n04 (2007): 267–71. http://dx.doi.org/10.1142/s1793048007000519.

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The Protein Data Bank (PDB) is the most important depository of protein structural information, containing more than 45,000 deposited entries today. Because of its inhomogeneous structure, its fully automated processing is almost impossible. In a previous work, we cleaned and re-structured the entries in the Protein Data Bank, and from the result we have built the RS-PDB database. Using the RS-PDB database, we draw a Ramachandran-plot from 6,593 "perfect" polypeptide chains found in the PDB, containing 1,192,689 residues. This is a more than tenfold increase in the size of data analyzed before
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4

Srinivasan, Narayanaswamy. "Chandrasekharan Ramakrishnan (1939–2019): The student behind the Ramachandran map." Protein Science 28, no. 11 (2019): 1920–22. http://dx.doi.org/10.1002/pro.3723.

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Pal, Debnath, and Pinak Chakrabarti. "On residues in the disallowed region of the Ramachandran map." Biopolymers 63, no. 3 (2002): 195–206. http://dx.doi.org/10.1002/bip.10051.

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6

Issa, Joseph B., Karsten Krogh-Jespersen, and Stephan S. Isied. "Conformational Dependence of Electronic Coupling Across Peptide Bonds: A Ramachandran Map." Journal of Physical Chemistry C 114, no. 48 (2010): 20809–12. http://dx.doi.org/10.1021/jp1071764.

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7

Malika, Bourjila, El Gridani Abderrahmane, Tijar Rachida, El Merbouh Brahim, and Drissi El Bouzaidi Rachid. "Theoretical investigation of Ramachandran plot of N-formyl-L-alanine-amide." Chemistry International 4, no. 4 (2018): 216–20. https://doi.org/10.5281/zenodo.1475389.

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The full conformational space of N-formyl-L-alanine-amide was explored by the semi-empirical method AM1 coupled to the Multi Niche Crowding (MNC) genetic algorithm implemented in a package of programs developed in our laboratory. The structural and energy analysis of the resulting conformational space E(,ψ) exhibits 5 regions or minima ɣL, ɣD, ɛL, D and αD. The technique provides better detection of local and global minima within a reasonable time.
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Siodłak, D., M. A. Broda, B. Rzeszotarska, A. E. Kozioł, and I. Dybała. "Conformational properties of N',N'-dimethylamides of N-acetyldehydroalanine and N-acetyl-(Z)-dehydrophenylalanine." Acta Biochimica Polonica 48, no. 4 (2001): 1179–83. http://dx.doi.org/10.18388/abp.2001_3888.

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Conformational preferences of Ac-deltaAla-NMe2 and Ac-(Z)-deltaPhe-NMe2 were studied and compared with those of their monomethyl counterparts as well as with those of their saturated analogues. X-Ray data and energy calculations revealed a highly conservative conformation of the dehydro dimethylamides, which is located in a high-energy region of the Ramachandran map.
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9

Mowbray, Sherry L., Charlotte Helgstrand, Jill A. Sigrell, Alexander D. Cameron, and T. Alwyn Jones. "Errors and reproducibility in electron-density map interpretation." Acta Crystallographica Section D Biological Crystallography 55, no. 7 (1999): 1309–19. http://dx.doi.org/10.1107/s0907444999005211.

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Three investigators, with varying levels of experience, independently built and refined the structure of Escherichia coli ribokinase at 2.6 Å resolution. At the end of the refinement/rebuilding processes the models had essentially converged, although each had its own particular pattern of remaining errors. The subsequent refinement of the same structure at 1.8 Å resolution allowed an overall quality check of each of the lower resolution models, and an analysis of which graphics-based tools were generally most efficient in locating these errors. Criteria which are useful in the application of R
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10

Kumar, Mayank, та R. S. Rathore. "RamPlot: a webserver to draw 2D, 3D and assorted Ramachandran (φ, ψ) maps". Journal of Applied Crystallography 58, № 2 (2025): 630–36. https://doi.org/10.1107/s1600576725001669.

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The Ramachandran steric map of torsion angles (φ, ψ) introduced in 1963 has been widely used for protein structure validation and model building. Many developments in the field have made it essential to develop a utility to plot assorted types of maps for the following specific reasons: (i) to investigate different types (Gly, Val/Ile, pre/trans/cis-Pro and general) of 2D and 3D maps, addressing the diverse steric environments and frequency distribution of conformations, (ii) to examine polypeptides containing non-standard residues, (iii) for better visualization and analysis of conformational
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Dissertations / Theses on the topic "Ramachandran Map"

1

Das, Chittaranjan. "Designed β-Hairpin, β-Sheet And Mixed α-β Structures In Synthetic Peptides". Thesis, Indian Institute of Science, 2000. https://etd.iisc.ac.in/handle/2005/263.

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Synthetic construction of protein molecules has been widely pursued over the last two decades. A primary goal behind de novo protein design has been to build minimal systems by capturing the essential features of protein structures. Such minimal models can be used to understand underlying principles governing folding, structure, and function of proteins molecules. Several approaches envisioning successful construction of synthetic proteins have been described over the years, some of them being admirably successful (DeGrado et al, 1999; Richardson et al> 1992; Baltzer, 1998). Specific patternin
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Das, Chittaranjan. "Designed β-Hairpin, β-Sheet And Mixed α-β Structures In Synthetic Peptides". Thesis, Indian Institute of Science, 2000. http://hdl.handle.net/2005/263.

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Synthetic construction of protein molecules has been widely pursued over the last two decades. A primary goal behind de novo protein design has been to build minimal systems by capturing the essential features of protein structures. Such minimal models can be used to understand underlying principles governing folding, structure, and function of proteins molecules. Several approaches envisioning successful construction of synthetic proteins have been described over the years, some of them being admirably successful (DeGrado et al, 1999; Richardson et al> 1992; Baltzer, 1998). Specific patternin
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3

DasGupta, Debarati. "Compuatational studies on tertiary structure prediction of small protiens and energetics of folding." Thesis, 2018. http://localhost:8080/iit/handle/2074/7627.

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Books on the topic "Ramachandran Map"

1

Biomolecular Forms and Functions: A Celebration of 50 Years of the Ramachandran Map. World Scientific Publishing Co Pte Ltd, 2012.

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2

Biomolecular Forms and Functions: A Celebration of 50 Years of the Ramachandran Map. World Scientific Publishing Co Pte Ltd, 2012.

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3

Srinivasan, N., and Manju Bansal. Biomolecular Forms and Functions: A Celebration of 50 Years of the Ramachandran Map. World Scientific Publishing Co Pte Ltd, 2012.

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4

Les, Alin. Despre minciuna. Ratiuni sociale, psihanalitice, spirituale, etice, criminologic-judiciare. Editura Universitara, 2020. http://dx.doi.org/10.5682/9786062811914.

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Faptul ca am ales sa scriu despre minciuna nu este aleator. Scriu despre minciuna pentru ca vreau sa contribui la o viata mai buna pentru semenii mei. Stiu ca daca nu reusesti sa o identifici, iti va fi dificil sa o probezi. Este important sa traiesti cat mai curat, dar si sa fi trecut prin perioade in care ai mintit. Minciuna nu poate fi inteleasa de la un amfiteatru virtual de unde se dau lectii de morala si etica. Dar o minciuna morala poate fi inteleasa daca intelegi ca minciuna este una dintre fantomele din creier („Fantomele din creier” este una din cartile lui V.S. Ramachandran scrisa i
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Book chapters on the topic "Ramachandran Map"

1

Da Rocha, Wagner, Carlile Lavor, Leo Liberti, and Thérèse E. Malliavin. "Pseudo-dihedral Angles in Proteins Providing a New Description of the Ramachandran Map." In Lecture Notes in Computer Science. Springer Nature Switzerland, 2023. http://dx.doi.org/10.1007/978-3-031-38299-4_53.

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2

Burton, James. "The Animal That Laughs at Itself." In Errans. ICI Berlin Press, 2022. http://dx.doi.org/10.37050/ci-24_2.

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A trio of themes recur across prominent Western theories of laughter: violence, the human/nonhuman, and error. The paper traces this trio through a series of frequently cited paradigms for understanding laughter, including superiority, incongruity and relief theories, Henri Bergson’s theory of laughter and V. S. Ramachandran’s false alarm theory; and argues that it reflects a shared, if partially submerged concern with the instability and demise of a particular figure of the human, one that is circumscribed by the culturally specific (if globally influential) values of Eurocentric/Western thou
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3

SHAPOVALOV, MAXIM V., and ROLAND L. DUNBRACK. "NON-PARAMETRIC STATISTICAL ANALYSIS OF THE RAMACHANDRAN MAP." In Biomolecular Forms and Functions. WORLD SCIENTIFIC / INDIAN INST OF SCIENCE, INDIA, 2013. http://dx.doi.org/10.1142/9789814449144_0006.

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LAKSHMI, B., G. ARCHUNAN, and N. SRINIVASAN. "PROPENSITIES OF AMINO ACID RESIDUES IN PROTEINS FOR DIFFERENT REGIONS OF THE RAMACHANDRAN MAP." In Biomolecular Forms and Functions. WORLD SCIENTIFIC / INDIAN INST OF SCIENCE, INDIA, 2013. http://dx.doi.org/10.1142/9789814449144_0010.

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5

BHAT, CHANDA R., MOITRAYEE BHATTACHARYYA, and SARASWATHI VISHVESHWARA. "NON-GLYCINE RESIDUES IN THE DISALLOWED REGIONS OF THE RAMACHANDRAN MAP AND THEIR NEIGHBORHOOD PREFERENCES." In Biomolecular Forms and Functions. WORLD SCIENTIFIC / INDIAN INST OF SCIENCE, INDIA, 2013. http://dx.doi.org/10.1142/9789814449144_0007.

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6

Hassunuma, Renato Massaharu, and Wilson Massashiro Yonezawa. "Um Desafio no Ensino de Bioquímica O Mapa de Ramachandran pela Aprendizagem Baseada em Jogos." In A educação através da multiplicidade de olhares: saberes, desafios e reflexões. Editora Integrar, 2023. http://dx.doi.org/10.51189/integrar/59/118.

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You might also be interested in the extended bibliographies on the topic 'Ramachandran Map' for particular source types:
Journal articles
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