Ministry of Education
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Dr Md Khurshid Alam Khan

vidwan id: 278530
Male

Associate Professor, Crescent School of Life Science
B S Abdur Rahman Crescent Institute of Science & Technology, Kancheepuram

Orchid Icon 0000-0002-3205-0729 Google Scholar Icon 55550454200 Google Scholar Icon 513jj4sAAAAJ

Expertise

  • Multidisciplinary Agriculture

Publications

Total Articles 32
Books 0
Proceedings 0

Publications

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Scopus

Citations 273
h-index 10

CrossRef

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Citations 280
h-index 11
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Professional Recognition

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Community & Membership

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Bio

Life Sciences

Personal Details

  • Male
  • Associate Professor , B S Abdur Rahman Crescent Institute of Science & Technology, Kancheepuram
  • B.S.Abdur Rahman Crescent Institute of Science and Technology, GST Road, Vandalur
PhD
Other Institute 2017
Associate Professor Jan 2014 – Present
B S Abdur Rahman Crescent Institute of Science & Technology, Kancheepuram | Crescent School of Life Science

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Co-Authors (14)

Mohammad

Prof Mohammad Afzal

Aligarh Muslim University

Asimul

Dr Asimul Islam

N/A

Arun Raj

Dr Arun Raj L

B S Abdur Rahman Crescent Institute of Science & Technology, Kancheepuram

Hemalatha

Dr Hemalatha S

B S Abdur Rahman Crescent Institute of Science & Technology, Kancheepuram

Faizan

Dr Faizan Ahmad

N/A

Karthika

Dr Karthika P

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Lavanya

Dr Lavanya V

Guru Nanak College (Autonomous)

Md. Imtaiyaz

Dr Md. Imtaiyaz Hassan

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Neesar

Dr Neesar Ahmed

B S Abdur Rahman Crescent Institute of Science & Technology, Kancheepuram

Rizwan Hasan

Prof Rizwan Hasan Khan

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Bharathidasan University

Alagiri

Dr Alagiri Srinivasan

Jamia Hamdard

Tanveer Ali

Dr Tanveer Ali Dar

University of Kashmir

Thirumurugan

Dr Thirumurugan D

S R M Institute of Science & Technology, Chennai

Scholarly Work

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Scholarly Publications

Conformational properties of polyglutamine sequences in guanidine hydrochloride solutions

Open Access
Article
Biophysical Journal. Year: 2012. Volume: 103 , Issue: 9 , Pages: 1989-1999 .
Authors: Khan M.;Bowler B.
DOI 10.1016/j.bpj.2012.09.041
2 2

Tryptophan Stabilizes His--Heme Loops in the Denatured State Only When It Is Near a Loop End

Open Access
article
Biochemistry. Year: 2012. Volume: 51 , Pages: 3586--3595 .
Authors: Khan, Md Khurshid A and Miller, Abbigail L and Bowler, Bruce E

Conformation and thermodynamic stability of pre-molten and molten globule states of mammalian cytochromes-c

Open Access
Review
Metallomics. Year: 2011. Volume: 3 , Issue: 4 , Pages: 327-338 .
Authors: Khan M.;Rahaman H.;Ahmad F.
DOI 10.1039/c0mt00078g
17 17

Conformational and thermodynamic characterization of the premolten globule state occurring during unfolding of the molten globule state of cytochrome c

Open Access
Article
Year: 2010. Volume: 15 , Issue: 8 , Pages: 1319-1329 .
Authors: Alam Khan M.K.;Rahaman M.H.;Hassan M.I.;Singh T.P.;Moosavi-Movahedi A.A.;Ahmad F.
DOI 10.1007/s00775-010-0691-5
28 28

A single mutation induces molten globule formation and a drastic destabilization of wild-type cytochrome c at pH 6.0

Open Access
Article
Year: 2009. Volume: 14 , Issue: 5 , Pages: 751-760 .
Authors: Khurshid Alam Khan M.;Das U.;Hamidur Rahaman M.;Imtaiyaz Hassan M.;Srinivasan A.;Singh T.P.;Ahmad F.
DOI 10.1007/s00775-009-0488-6
37 40

Sequence and stability of the goat cytochrome c

Open Access
Article
Biophysical Chemistry. Year: 2008. Volume: 138 , Issue: 1-2 , Pages: 23-28 .
Authors: Rahaman H.;Khan K.A.;Hassan I.;Wahid M.;Singh S.B.;Singh T.P.;Moosavi-Movahedi A.A.;Ahmad F.
DOI 10.1016/j.bpc.2008.08.008
17 17

Intermediate formation at lower urea concentration in ‘B’isomer of human serum albumin: a case study using domain specific ligands

Open Access
article
Biochemical and Biophysical Research Communications. Year: 2004.
Authors: Basir Ahmad, Mohd Khursheed Alam Khan, Soghra Khatun Haq, Rizwan Hasan Khan

Characterization of a partially folded intermediate of papain induced by fluorinated alcohols at low pH

Open Access
Article
Archives of Biochemistry and Biophysics. Year: 2004. Volume: 432 , Issue: 1 , Pages: 79-87 .
Authors: Naeem A.;Khan K.;Khan R.
DOI 10.1016/j.abb.2004.08.019
33 39