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{{Use British English|date=March 2013}}
{{Use dmy dates|date=March 2013}}
{{Infobox scientist
|name = Mamannamana Vijayan
|image =
|image_size =
|caption =
|birth_date = 16 Oct 1941
|birth_place = [[Cherpu]], Kerala
|death_date =
|death_place =
|residence = [[Bangalore]]
|citizenship =
|nationality = [[India]]n
|ethnicity =
|field = [[Biological sciences]]
|work_institution = [[Indian Institute of Science]] 
|alma_mater = [[Indian Institute of Science]]
|doctoral_advisor = [[Mysore A. Viswamitra]]
|doctoral_students =
|known_for = [[Protein crystallography]]
|author_abbrev_bot =
|author_abbrev_zoo =
|influences =
|influenced =
|prizes = [[Padma Shri]] (2004), [[Shanti Swarup Bhatnagar Prize for Science and Technology]](1985)
|religion =
|footnotes =
|signature =
}}

'''Mamannamana Vijayan''' (born 16 October 1941, [[Cherpu]], Kerala<ref name="bio_iac">{{Cite web|title=About M. Vijayan|url=http://www.interacademycouncil.net/?id=10080|publisher=[[InterAcademy Council]]|year=2003|access-date=20 September 2010}}</ref>) is an Indian structural biologist. His main area of research is [[protein]] structures. His contributions have been towards the structure and carbohydrate specificity of [[lectins]] and [[protein]] hydration. He has also contributed towards the area of structure and interactions of mycobacterial proteins and [[supramolecular]] association with reference to chemical evolution and [[Abiogenesis|origin of life]]. Vijayan did [[Crystallography#Biology|biological macromolecular crystallography]] in India.<ref name="bio_iac" />

He was awarded [[Padma Shri]] by the [[President of India]] in 2004.<ref name="padmashri">{{Cite web|url=http://india.gov.in/myindia/padmashri_awards_list1.php?start=540|title=Padma Shri Awardees|publisher=[[Government of India]]|year=2005|access-date=2010-09-12}}</ref> He was the President of the [[Indian National Science Academy]] from 2007–2010.<ref name="insa">{{Cite web|url=http://www.insaindia.org/advisory.htm |archive-url=https://archive.is/20130415031938/http://www.insaindia.org/advisory.htm |url-status=dead |archive-date=15 April 2013 |title=About INSA: Advisory Committees for the Year 2010 |access-date=20 September 2010 |publisher=India National Science Society }}</ref> Currently, he is [[Department of Atomic Energy (India)|DAE]] Homi Bhabha Professor at the [[Indian Institute of Science]].

==Education==
Vijayan obtained his Masters of Science degree in 1963 from [[Allahabad University]]. Thereafter, he received his Doctorate degree in [[X-ray crystallography]] from the [[Indian Institute of Science]] in 1967. During 1968–71, he was a [[post-doctoral fellow]] in Professor [[Dorothy Hodgkin]]’s research group at [[University of Oxford]]. During that period, he studied x-ray diffraction data for [[insulin]] crystals.<ref>{{Cite journal|title=Structure of Rhombohedral 2 Zinc Insulin Crystals |last1=Adams |first1=M.J. |last2=Blundell |first2=T.L. |last3=Dodson |first3=E.J. |last4=Dodson |first4=G.G. |last5=Vijayan |first5=M. |last6=Baker |first6=E.N. |last7=Harding |first7=M.M. |last8=Hodgkin |first8=D.C. |last9=Rimmer |first9=B. |last10=Sheat |first10=S. |volume=224 |issue= 5218|pages=491–495 |journal=[[Nature (journal)|Nature]] |date=1 November 1969 |doi=10.1038/224491a0|bibcode = 1969Natur.224..491A |s2cid=4216737 |display-authors=8 }}</ref>

==Contribution in structural biology==
Vijayan's students and postdocs have dealt with four of the five structural classes of plant lectins. They have studied in detail lectins from peanut, [[winged bean]] (basic and acidic), [[jackfruit]] ([[jacalin]] and artocarpin), garlic, banana and [[snake gourd]]. The work on lectins demonstrated the need for considering open quaternary structures when dealing with multimeric proteins<ref>{{Cite journal|title=Crystal structure of peanut lectin, a protein with an unusual quaternary structure |last1=Banerjee |first1=R. |last2=Mande |first2=S.C. |last3=Ganesh |first3=V. |last4=Das |first4=K. |last5=Dhanaraj |first5=V. |last6=Mahanta |first6=S.K. |last7=Suguna |first7=K. |last8=Surolia |first8=A. |last9=Vijayan |first9=M. |volume=91 |issue=1 |date=4 January 1994 |pages=227–231|pmid=8278370|pmc=42920|journal=Proceedings of the National Academy of Sciences |bibcode = 1994PNAS...91..227B |doi = 10.1073/pnas.91.1.227 }}</ref> and the variability in the quaternary association of legume lectins.<ref>{{Cite journal|last1=Prabu |first1=M.M. |last2=Sankaranarayanan |first2=R. |last3=Puri |first3=K.D. |last4=Sharma |first4=V. |last5=Surolia |first5=A. |last6=Vijayan |first6=M. |last7=Suguna |first7=K. |title=Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution |date=6 March 1998 |volume=276 |issue=4 |pages=787–96 | pmid=9500920|doi=10.1006/jmbi.1997.1568|journal=Journal of Molecular Biology }}</ref><ref>{{Cite journal|title=Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins |last1=Prabu |first1=M.M. |last2=Suguna |first2=K. |last3=Vijayan |first3=M. |date=1 April 1999 |volume=35 |issue=1 |pages=58–69 | pmid= 10090286|doi=10.1002/(SICI)1097-0134(19990401)35:1<58::AID-PROT6>3.0.CO;2-A|journal=Proteins|doi-access=free }}</ref><ref>{{Cite journal|title=Effect of glycosylation on the structure of Erythrina corallodendron lectin |last1=Kulkarni |first1=K.A. |last2=Srivastava |first2=A. |last3=Mitra |first3=N. |last4=Sharon |first4=N. |last5=Surolia |first5=A. |last6=Vijayan |first6=M. |last7=Suguna |first7=K. |date=1 September 2004 |volume=56 |issue=4 |pages=821–7| pmid = 15281133|doi=10.1002/prot.20168|journal=Proteins |s2cid=19291744 }}</ref> and lectins with the β-prism I fold.<ref>{{Cite journal|title=Unusual sugar specificity of banana lectin from Musa paradisiaca and its probable evolutionary origin. Crystallographic and modelling studies |last1=Singh |first1=D.D. |last2=Saikrishnan |first2=K. |last3=Kumar |first3=P. |last4=Surolia |first4=A. |last5=Sekar |first5=K. |last6=Vijayan |first6=M. |date = October 2005|volume=15 |issue=10 |pages=1025–32 | pmid= 15958419|doi=10.1093/glycob/cwi087|journal=Glycobiology |doi-access=free }}</ref> His group established β-prism I fold as a lectin fold.<ref>{{Cite journal|title=A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold |last1=Sankaranarayanan |first1=R. |last2=Sekar |first2=K. |last3=Banerjee |first3=R. |last4=Sharma |first4=V. |last5=Surolia |first5=A. |last6=Vijayan |first6=M.
|date = July 1996|volume=3 |issue=7 |pages=596–603| pmid = 8673603|journal=Nature Structural Biology |doi=10.1038/nsb0796-596|s2cid=23593928 }}</ref> They explained the roles of water-bridges, post-translational modification, [[oligomerisation]] and variation in loop length as strategies for generating ligand specificity.<ref>{{Cite journal|title=Crystal structure of the peanut lectin – T-antigen complex. Carbohydrate specificity generated by water bridges |last1=Ravishankar |first1=R. |last2=Ravindran |first2=M. |last3=Suguna |first3=K. |last4=Surolia |first4=A. |last5=Vijayan |first5=Vijayan |journal=Current Science |volume=72 |issue=11 |date=10 June 1997 |access-date=20 September 2010 |url=http://www.ias.ac.in/j_archive/currsci/72/11/855-861/viewpage.html}}</ref><ref>{{Cite journal|title=Structural basis for the energetics of jacalin-sugar interactions: promiscuity versus specificity |last1=Arockia Jeyaprakash |first1=A. |last2=Jayashree |first2=G. |last3=Mahanta |first3=S.K. |last4=Swaminathan |first4=C.P. |last5=Sekar |first5=K. |last6=Surolia |first6=A. |last7=Vijayan |first7=M. |date=18 March 2005 |volume=347 |issue=1 |pages=181–188 | pmid= 15733927|doi=10.1016/j.jmb.2005.01.015|journal=Journal of Molecular Biology }}</ref><ref>{{Cite journal|title=Crystal structure of a dimeric mannose-specific agglutinin from garlic: Quaternary association and carbohydrate specificity |last1=Chandra |first1=N.R. |last2=Ramachandraiah |first2=G. |last3=Bachhawat |first3=K. |last4=Dam |first4=T.K. |last5=Surolia |first5=A. |last6=Vijayan |first6=M. |date=22 January 1999 |volume=285 |issue=3 |pages=1157–68| pmid = 9887270|doi=10.1006/jmbi.1998.2353|journal=Journal of Molecular Biology }}</ref><ref>{{Cite journal|title=Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin |last1=Manoj |first1=N. |last2=Srinivas |first2=V.R. |last3=Surolia |first3=A. |last4=Vijayan |first4=M. |last5=Suguna |first5=K. |date=6 October 2000 |volume=302 |issue=5 |pages=1129–37| pmid = 11183779|doi=10.1006/jmbi.2000.4111|journal=Journal of Molecular Biology }}</ref><ref>{{Cite journal|title=Structural basis for the carbohydrate specificities of artocarpin: Variation in the length of a loop as a strategy for generating ligand specificity |last1=Jeyaprakash |first1=A.A. |last2=Srivastav |first2=A. |last3=Surolia |first3=A. |last4=Vijayan |first4=M. |date=7 May 2004 |volume=338 |issue=4 |pages=757–770| pmid = 15099743|doi=10.1016/j.jmb.2004.03.040|journal=Journal of Molecular Biology |citeseerx=10.1.1.530.4331 }}</ref><ref>{{Cite journal|title=Lectins |last1=Vijayan |first1=M. |last2=Chandra |first2=N. |date=9 December 1999 |volume=9 |issue=6 |pages=707–714| pmid = 10607664|journal=Current Opinion in Structural Biology |doi=10.1016/S0959-440X(99)00034-2}}</ref> Their studies provided insights into the structural basis of carbohydrate specificity and the biological implications of this specificity.<ref>{{Cite journal|title=Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex |last1=Banerjee |first1=R.|last2=Das|first2=K.|last3=Ravishankar |first3=R. |last4=Suguna |first4=K. |last5=Surolia |first5=A. |last6=Vijayan |first6=M. |date=7 June 1996 |volume=259 |issue=2 |pages=281–296| pmid = 8656429|doi=10.1006/jmbi.1996.0319|journal=Journal of Molecular Biology |citeseerx=10.1.1.335.6342 }}</ref><ref>{{Cite journal|title=Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-alpha-D-mannose: implications to the generation of carbohydrate specificity |last1=Pratap |first1=J.V. |last2=Jeyaprakash |first2=A.A. |last3=Rani |first3=P.G. |last4=Sekar |first4=K.|last5=Surolia |first5=A.|last6=Vijayan |first6=M. |date=22 March 2001 |volume=317 |issue=2 |pages=237–247| pmid = 11902840|doi=10.1006/jmbi.2001.5432|journal=Journal of Molecular Biology }}</ref><ref>{{Cite journal|title=Computational analysis of multivalency in lectins: Structures of garlic lectin-oligosaccharide complexes and their aggregates |last1=Ramachandraiah |first1=G.|last2=Chandra |first2=N.R.|last3=Surolia |first3=A.|last4=Vijayan |first4=M. |date=November 2003 |volume=13 |issue=11 |pages=765–75 | pmid= 12851290|doi=10.1093/glycob/cwg095|journal=Glycobiology|doi-access=free }}</ref><ref>{{Cite journal|title=Generation of blood group specificity: New insights from structural studies on the complexes of A- and B-reactive saccharides with basic winged bean agglutinin |last1=Kulkarni |first1=K.A. |last2=Katiyar |first2=S.|last3=Surolia |first3=A.|last4=Vijayan |first4=M.|last5=Suguna|first5=K. |date=15 August 2007 |volume=68 |issue=3 |pages=762–769| pmid = 17510954|doi=10.1002/prot.21428|journal=Proteins |s2cid=38438194 }}</ref><ref>{{Cite journal|last1=Kundhavai Natchiar |first1=S.|last2=Suguna |first2=K.|last3=Surolia |first3=A. |last4=Vijayah |first4=M. |title=Peanut agglutinin, a lectin with an unusual quaternary structure and interesting ligand binding properties |journal=Crystallography Reviews |year=2007 |issue=13 |pages=1–26}}</ref><ref>{{Cite journal|title=Structure, dynamics, and interactions of jacalin. Insights from molecular dynamics simulations examined in conjunction with results of X-ray studies |last1=Sharma |first1=A. |last2=Sekar |first2=K. |last3=Vijayan |first3=M. |date = December 2009|volume=77 |issue=4 |pages=760–77| pmid = 19544573|doi=10.1002/prot.22486|journal=Proteins |s2cid=24614113 }}</ref> Using an approach involving water-mediated transformations, Vijayan's research determined the nature of the flexibility in [[lysozyme]] and [[ribonuclease A]] and identified the invariant features in their hydration shells.<ref>{{Cite journal|title=Crystal structure of low humidity tetragonal lysozyme at 2.1-A resolution. Variability in hydration shell and its structural consequences |last1=Kodandapani |first1=R.|last2=Suresh |first2=C.G. |last3=Vijayan |first3=M. |date=25 September 1990 |volume=265 |issue=27 |pages=16126–16131| pmid = 2398048|journal=Journal of Biological Chemistry |doi=10.2210/pdb4lym/pdb }}
</ref><ref>{{Cite journal|title=Water-dependent domain motion and flexibility in ribonuclease A and the invariant features in its hydration shell. An X-ray study of two low-humidity crystal forms of the enzyme |last1=Kishan |first1=R.V.|last2=Chandra |first2=N.R.|last3=Sudarsanakumar |first3=C.|last4=Suguna |first4=K.|last5=Vijayan |first5=M. |date=1 September 1995 |volume=51 |pages=703–10| pmid = 15299799|issue=Pt 5|doi=10.1107/S0907444994014794|journal=Acta Crystallographica D |url=http://journals.iucr.org/d/issues/1995/05/00/se0153/se0153.pdf}}</ref><ref>{{Cite journal |last1=Nagendra |first1=H.G.|last2=Sukumar |first2=N.|last3=Vijayan |first3=M. |date=1 August 1998 |volume=32 |issue=2 |pages=229–240 |title=Role of water in plasticity, stability, and action of proteins: The crystal structures of lysozyme at very low levels of hydration| pmid = 9714162 |doi=10.1002/(SICI)1097-0134(19980801)32:2<229::AID-PROT9>3.0.CO;2-F |journal=Proteins }}</ref> His research also demonstrated the presence of ensembles of relaxed and tense states of haemoglobin.<ref>{{Cite journal|title=A new relaxed state in horse methemoglobin characterized by crystallographic studies |last1=Sankaranarayanan |first1=R.|last2=Biswal |first2=B.K.|last3=Vijayan |first3=M. |date=15 August 2005 |volume=60 |issue=3 |pages=547–51| pmid = 15887226|doi=10.1002/prot.20510|journal=Proteins |citeseerx=10.1.1.556.8763 |s2cid=34532239 }}</ref> and water-mediated loop movement in β-lactoglobulin.<ref>{{Cite journal|title=An asymmetric dimer of beta-lactoglobulin in a low humidity crystal form – structural changes that accompany partial dehydration and protein action |last1=Vijayalakshmi |first1=L.|last2=Krishna |first2=R.|last3=Sankaranarayanan |first3=R.|last4=Vijayan |first4=M. |date = April 2008|volume=71|issue=1 |pages=241–249| pmid = 17932936|doi=10.1002/prot.21695|journal=Proteins |s2cid=26828581 }}</ref> His studies have provided insights into the relationship among hydration, molecular mobility and protein action.

Vijayan organised a national programme on the structural biology of microbial pathogens. His research in the area has been concerned with mycobacterial, particularly [[tuberculosis]], related proteins. The specific systems studied by him include [[RecA]], RuvA, uracil DNA glycosylase, single stranded DNA binding protein, ribosome recycling factor, peptidyl tRNA hydrolase, pantothenate kinase and DNA binding protein in stationary phase cells.<ref>{{Cite journal|title=Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): Implications for decreased ATPase activity and molecular aggregation |last1=Datta |first1=S.|last2=Prabu |first2=M.M.|last3=Vaze |first3=M.B.|last4=Ganesh |first4=N.|last5=Chandra |first5=N.R. |last6=Muniyappa |first6=K.|last7=Vijayan |first7=S. |date=15 December 2000 |volume=28|issue=24 |pages=4964–4973| pmid = 11121488|pmc=115232|journal=Nucleic Acids Research |doi=10.1093/nar/28.24.4964}}</ref><ref>{{Cite journal|title=Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications |last1=Saikrishnan |first1=K.|last2=Jeyakanthan |first2=J.|last3= Venkatesh|first3=J.|last4=Acharya |first4=N.|last5=Sekar |first5=K.|last6=Varshney |first6=U.|last7=Vijayan |first7=M. |date=8 August 2003 |volume=331 |issue=2 |pages=385–93| pmid = 12888346|journal=Journal of Molecular Biology |doi=10.1016/S0022-2836(03)00729-0|citeseerx=10.1.1.726.1605 }}</ref><ref>{{Cite journal|title=X-ray structural studies of Mycobacterium tuberculosis RRF and a comparative study of RRFs of known structure. Molecular plasticity and biological implications |last1=Saikrishnan |first1=K.|last2=Kalapala|first2=S.K.|last3= Varshney|first3=U.|last4=Vijayan |first4=M. |date=7 January 2005 |volume=345|issue=1|pages=29–38| pmid = 15567408|doi=10.1016/j.jmb.2004.10.034|journal=Journal of Molecular Biology }}</ref><ref>{{Cite journal|title=Structural biology of mycobacterial proteins: The Bangalore effort |last=Vijayan |first=M. |year=2005 |volume=85 |issue=5–6 |pages=357–366 | pmid=16260182|doi=10.1016/j.tube.2005.08.011|journal=Tuberculosis}}</ref><ref>{{Cite journal|title=Snapshots of RecA protein involving movement of the C-domain and different conformations of the DNA-binding loops: crystallographic and comparative analysis of 11 structures of Mycobacterium smegmatis RecA |last1=Krishna |first1=R.|last2=Prabu |first2=J.R.|last3=Manjunath |first3=G.P.|last4=Datta |first4=S.|last5=Chandra |first5=N.R. |last6=Muniyappa |first6=K.|last7=Vijayan |first7=M. |date=6 April 2007 |volume=367 |issue=4 |pages=1130–1144|pmid= 17306300|doi=10.1016/j.jmb.2007.01.058|journal=Journal of Molecular Biology }}</ref><ref>{{Cite journal|title=Structural plasticity and enzyme action: crystal structures of mycobacterium tuberculosis peptidyl-tRNA hydrolase |last1=Selvaraj |first1=M.|last2=Roy |first2=S.|last3=Singh|first3=N.S.|last4=Sangeetha|first4=R.|last5=Varshney |first5=U.|last6=Vijayan |first6=M. |date=7 September 2007 |volume=372 |issue=1 |pages=186–93 |pmid= 17619020|doi=10.1016/j.jmb.2007.06.053|journal=Journal of Molecular Biology }}</ref><ref>{{Cite journal|title=Structural studies on the second Mycobacterium smegmatis Dps: Invariant and variable features of structure, assembly and function |last1=Roy |first1=S.|last2=Saraswathi|first2=R.|last3=Chatterji |first3=D. |last4=Vijayan |first4=M. |date=25 January 2008 |volume=375 |issue=4 |pages=948–959 |pmid= 18061613|doi=10.1016/j.jmb.2007.10.023|journal=Journal of Molecular Biology }}</ref><ref>{{Cite journal|title=Unique features of the structure and interactions of mycobacterial uracil-DNA glycosylase: Structure of a complex of the Mycobacterium tuberculosis enzyme in comparison with those from other sources |last1=Kaushal |first1=P.S. |last2=Talawar |first2=R.K.|last3=Krishna |first3=P.D. |last4=Varshney |first4=U.|last5=Vijayan |first5=M. |date = May 2008|volume=64 |pages=551–560 |pmid=18453691|issue=Pt 5|doi=10.1107/S090744490800512X|journal=Acta Crystallographica D}}</ref><ref>{{Cite journal|title=Crystallographic and modelling studies on Mycobacterium tuberculosis RuvA: Additional role of RuvB-binding domain and inter species variability |last1=Prabu |first1=J.R. |last2=Thamotharan |first2=S.|last3=Khanduja |first3=J.S.|last4=Chandra |first4=N.R.|last5=Muniyappa |first5=K.|last6=Vijayan |first6=M.|date = July 2009|volume=1794 |issue=7 |pages=1001–1009 |pmid=19374958|doi=10.1016/j.bbapap.2009.04.003|journal=Biochimica et Biophysica Acta }}</ref><ref>{{Cite journal|title=M. tuberculosis pantothenate kinase: Dual substrate specificity and unusual changes in ligand locations |last1=Chetnani |first1=B.|last2=Kumar |first2=P.|last3=Surolia |first3=A.|last4=Vijayan |first4=M. |date=9 July 2010 |volume=400 |issue=2 |pages=171–185 | pmid=20451532|doi=10.1016/j.jmb.2010.04.064|journal=Journal of Molecular Biology }}</ref> He has elucidated the specific structural features of these proteins in mycobacteria, which, among other things, have opened up avenues for structure-based inhibitor design, with the eventual objective of drug development.

Vijayan's research have determined the molecular recognition and aggregation patterns involving amino acids and peptides using an approach based on molecular complexes. This has implications to chemical evolution and origins of life.<ref>{{Cite journal|title=Molecular interactions and aggregation involving amino acids and peptides and their role in chemical evolution |last=Vijayan |first=M. |year=1988 |volume=52 |issue=2 |pages=71–99 | pmid=3076685|journal=Progress in Biophysics and Molecular Biology |doi=10.1016/0079-6107(88)90003-X|doi-access=free }}</ref><ref>{{Cite journal|title=X-ray studies of crystalline complexes involving amino acids and peptides. XLIV. Invariant features of supramolecular association and chiral effects in the complexes of arginine and lysine with tartaric acid |last1=Selvaraj |first1=M.|last2=Thamotharan |first2=S.|last3=Roy |first3=S.|last4=Vijayan |first4=M. |date = June 2007|volume=63 |pages=459–68 | pmid= 17507759|issue=Pt 3|doi=10.1107/S010876810701107X|journal=Acta Crystallographica B}}</ref> His other contributions pertain to the structure and interactions of non-steroidal anti-inflammatory analgesics,<ref>{{Cite journal|title=Structural studies of analgesics and their interactions. Part 4. Crystal structures of phenylbutazone and a 2 : 1 complex between phenylbutazone and piperazine |last1=Singh |first1=Tej Pal |last2=Vijayan |first2=Mamannamana |year=1977 |volume=2 |pages=693–699 |doi=10.1039/P29770000693|journal=Journal of the Chemical Society, Perkin Transactions 2|issue=5}}</ref> ionophores and related compounds,<ref>{{Cite journal|title=A novel conformation of valinomycin in its barium complex |last1=Devarajan |first1=S. |last2=Nair |first2=C.M.K. |author3-link=K. R. K. Easwaran |last3=Easwaran |first3=K.R.K. |last4=Vijayan |first4=M. |volume= 286 |pages=640–641 |date=7 August 1980 |doi=10.1038/286640a0 |issue=5773|journal=Nature|pmid=7402346|bibcode = 1980Natur.286..640D |s2cid=4319387 }}</ref> side chain conformation in proteins<ref>{{Cite journal|title=An analysis of side-chain conformation in proteins |last1=Bhat |first1=T.N. |last2=Sasisekharan |first2=V.|last3=Vijayan |first3=M. |date = February 1979|volume=13 |issue=2 |pages=170–84| pmid = 429093|journal=International Journal of Peptide and Protein Research|doi=10.1111/j.1399-3011.1979.tb01866.x }}</ref> and additional binding sites in lysozyme.<ref>{{Cite journal|title=Additional binding sites in lysozyme. X-ray analysis of lysozyme complexes with bromophenol red and bromophenol blue |last1=Madhusudan |last2=Vijayan |first2=M. |date = July 1992|volume=5|issue=5|pages=399–404| pmid = 1518787|journal=Protein Engineering |doi=10.1093/protein/5.5.399}}</ref>

Vijayan has published more than 260 peer reviewed research articles and has guided 38 research students and 20 postdoctoral fellows.<ref name="bio_iac" />

==Professional life==
After completing his postdoctoral research at the University of Oxford, he returned to India in 1971 and joined the Molecular Biophyiscs Unit at the [[Indian Institute of Science]] (IISc). He has served in various capacities such as Professor, Chairman of Molecular Biophysics Unit, Chairman of Division of Biological Sciences among others. During 2000–2004 he was Associate Director of IISc.<ref name="bio_iac" /> He has continued to work at the Institute as a DBT Distinguished Biotechnologist and subsequently as a DAE Homi Bhabha Professor.

Prof. Vijayan's course on fundamentals in crystallography was extremely popular with students at the Indian Institute of Science. His unique approach of interlacing historical developments in the field with conceptual aspects made the course vibrant and energetic.<ref>{{Cite journal|last=Srinivasan|first=Bharath|date=2020-09-27|title=Words of advice: teaching enzyme kinetics|url=http://dx.doi.org/10.1111/febs.15537|journal=The FEBS Journal|doi=10.1111/febs.15537|issn=1742-464X|doi-access=free}}</ref>

==Role in international and national organisations==
Vijayan is a member of the [[International Union of Crystallography]] (IUCr), the International Union of Pure & Applied Biophysics (IUPAB), the International Council for Science (ICSU), the Inter Academy Panel (IAP) and the [[InterAcademy Council]] (IAC). He is a former president of the Asian Crystallographic Association.<ref name="bio_iac" /> He has been involved in the activities of the science departments and agencies of the [[Government of India]] and different scientific institutions in the country. He is the Founder President of the Indian Crystallographic Association<ref>{{Cite web|url=http://iris.physics.iisc.ernet.in/ica/past.html |title=Past Office Bearers – Year (2001–2003) |publisher=Indian Crystallographic Association |access-date=20 September 2010}}</ref> and has served as the President of the Indian Biophysical Society and the President of the Indian National Science Academy (2007–2010).<ref name="insa"/>

==Awards and recognitions==
Vijayan is a Fellow of the three science academies of India<ref name="bio_iac" /> and the Academy of Sciences for the Developing World ([[TWAS]]).<ref>{{Cite web|url=http://twas.ictp.it/mbrs/mbrs-section/02 |title=Members: Structural, Cell and Molecular Biology |access-date=20 September 2010 |publisher=TWAS |url-status=dead |archive-url=https://web.archive.org/web/20110722035743/http://twas.ictp.it/mbrs/mbrs-section/02 |archive-date=22 July 2011 }}</ref> He has won the [[Shanti Swarup Bhatnagar Prize]], GN Ramachandran Medal by INSA, Alumni Award Excell. Res. by IISc, FICCI Award Life Sci., Ranbaxy Res. Award by Basic Medical Sciences, JL Nehru Centen. vis. fellow by INSA, Om Prakash Bhasin Award, KS Krishnan Memorial Lecture by INSA, JL Nehru Birth Centen. Award by Indian Science Congress Assoc., [[Padma Shri]],<ref name="padmashri"/> Distinguished Biotechnologist Award by DBT; Goyal Prize, first CSIR/Science Congress GN Ramachandran Award for Excellence in Biological Science and Technology, Distinguished Alumni Award and Lakshmipat Singhania-[[IIM Lucknow]] National Leadership Award for Science and Technology-Leader, 2009.

==References==
{{Reflist|colwidth=30em}}

==External links==
* [https://web.archive.org/web/20120307125846/http://www.biomedexperts.com/Profile.bme/1486846/Mamannamana_Vijayan M. Vijayan profile on Biomed Experts]
* [http://en.scientificcommons.org/mamannamana_vijayan Mamannamana Vijayan publications list]
* [http://mbu.iisc.ernet.in/~mvlab/ M. Vijayan home page at Indian Institute of Science]

{{Padma Shri Award Recipients in Science & Engineering}}
{{Padma Award winners of Kerala}}
{{SSBPST recipients in Biological Science}}
{{Shanti Swarup Bhatnagar Laureates of Kerala}}
{{Authority control}}

{{DEFAULTSORT:Vijayan, Mamannamana}}
[[Category:1941 births]]
[[Category:Living people]]
[[Category:Recipients of the Padma Shri in science & engineering]]
[[Category:Scientists from Bangalore]]
[[Category:Alumni of the University of Oxford]]
[[Category:Fellows of the Indian National Science Academy]]
[[Category:20th-century Indian biologists]]
[[Category:Scientists from Kerala]]
[[Category:People from Thrissur district]]
[[Category:University of Allahabad alumni]]
[[Category:Indian Institute of Science alumni]]
[[Category:Indian Institute of Science faculty]]
[[Category:Recipients of the Shanti Swarup Bhatnagar Award in Biological Science]]

M. Vijayan - Revision history

imported>DontWannaDoThis at 06:31, 21 August 2021