TY  - CHAP
M1  - Book, Section
TI  - Proteins: Higher Orders of Structure
A1  - Kennelly, Peter J.
A1  - Rodwell, Victor W.
A2  - Rodwell, Victor W.
A2  - Bender, David A.
A2  - Botham, Kathleen M.
A2  - Kennelly, Peter J.
A2  - Weil, P. Anthony
PY  - 2018
T2  - Harper's Illustrated Biochemistry, 31e
AB  - OBJECTIVESAfter  studying  this  chapter,  you  should  be  able  to:Indicate  the  advantages  and  drawbacks  of  several  approaches  to  classifying  proteins.Explain  and  illustrate  the  primary,  secondary,  tertiary,  and  quaternary  structure  of  proteins.Identify  the  major  recognized  types  of  secondary  structure  and  explain  supersecondary  motifs.Describe  the  kind  and  relative  strengths  of  the  forces  that  stabilize  each  order  of  protein  structure.Describe  the  information  summarized  by  a  Ramachandran  plot.Summarize  the  basic  operating  principles  underlying  three  key  methods  for  determining  protein  structure:  X-ray  crystallography,  nuclear  magnetic  resonance  spectroscopy,  and  cryo-electron  microscopy.Indicate  the  present  state  of  knowledge  concerning  the  stepwise  process  by  which  proteins  are  thought  to  attain  their  native  conformation.Identify  the  physiologic  roles  in  protein  maturation  of  chaperones,  protein  disulfide  isomerase,  and  peptidylproline  cis–trans  isomerase.Describe  the  principal  biophysical  techniques  used  to  study  tertiary  and  quaternary  structure  of  proteins.Explain  how  genetic  and  nutritional  disorders  of  collagen  maturation  illustrate  the  close  linkage  between  protein  structure  and  function.For  the  prion  diseases,  outline  the  overall  events  in  their  molecular  pathology  and  name  the  life  forms  each  affects.  
SN  - 
PB  - McGraw-Hill Education
CY  - New York, NY
Y2  - 2024/04/19
UR  - accesspharmacy.mhmedical.com/content.aspx?aid=1160188794
ER  -