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00000cam a2200000Ma 4500 |
001 |
SCIDIR_ocn711568867 |
003 |
OCoLC |
005 |
20231117044601.0 |
006 |
m o d |
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cr cn||||||||| |
008 |
110304s1997 caua ob 001 0 eng d |
040 |
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|a SFB
|b eng
|e pn
|c SFB
|d OCLCQ
|d OPELS
|d OCLCQ
|d OPELS
|d OCLCF
|d OCLCQ
|d DEBSZ
|d UAB
|d D6H
|d CHVBK
|d LEAUB
|d UHL
|d OCLCA
|d UK7LJ
|d LUN
|d S2H
|d OCLCO
|d OCLCQ
|d INARC
|d OCLCQ
|d OCLCO
|d OCLCQ
|
019 |
|
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|a 1113040382
|a 1127161564
|a 1136485410
|a 1144288912
|a 1156170518
|a 1162084954
|a 1244029840
|a 1280779031
|
020 |
|
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|a 0120342502
|q (electronic bk.)
|
020 |
|
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|a 9780120342501
|q (electronic bk.)
|
035 |
|
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|a (OCoLC)711568867
|z (OCoLC)1113040382
|z (OCoLC)1127161564
|z (OCoLC)1136485410
|z (OCoLC)1144288912
|z (OCoLC)1156170518
|z (OCoLC)1162084954
|z (OCoLC)1244029840
|z (OCoLC)1280779031
|
050 |
|
4 |
|a QD431
|b .A3 v. 50 1997
|
082 |
0 |
4 |
|a 572.633
|
084 |
|
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|a 35.75
|2 bcl
|
245 |
0 |
0 |
|a Protein misassembly /
|c edited by Ronald Wetzel.
|
260 |
|
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|a San Diego :
|b Academic Press,
|c �1997.
|
300 |
|
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|a 1 online resource (xx, 282 pages) :
|b illustrations (some color).
|
336 |
|
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|a text
|b txt
|2 rdacontent
|
337 |
|
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|a computer
|b c
|2 rdamedia
|
338 |
|
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|a online resource
|b cr
|2 rdacarrier
|
490 |
1 |
|
|a Advances in protein chemistry,
|x 0065-3233 ;
|v v. 50
|
504 |
|
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|a Includes bibliographical references and indexes.
|
505 |
0 |
|
|a Protein misassembly in vitro / Rainer Jaenicke and Robert Seckler -- Oligomer Formation by 3D domain swapping: a model for protein assembly and misassembly / Michael P. Schlunegger, Melanie J. Bennett, and David Eisenberg -- The structure of amyloid fibrils by electron microscopy and x-ray diffraction / Margaret Sunde andColin Blake -- Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid / Jeffery W. Kelly ... et al. -- Domain stability in immunoglobulin light chain deposition disorders / Ronald Wetzel -- Mutational effects on inclusion body formation / Scott Betts, Cameron Haase-Pettingell, and Jonathan King.
|
588 |
0 |
|
|a Print version record.
|
520 |
|
|
|a The role that primary amino acid sequences plays in influencing the partitioning of polypeptides between productive folding and irreversible aggregation pathways has introduced a whole new dimension to the folding problem. The volume deals with the structures of the products of protein misassembly and the role of amino acid sequences in favoring these structures.
|
650 |
|
0 |
|a Proteins
|x Conformation.
|
650 |
|
0 |
|a Protein folding.
|
650 |
|
2 |
|a Protein Folding
|0 (DNLM)D017510
|
650 |
|
2 |
|a Protein Conformation
|0 (DNLM)D011487
|
650 |
|
6 |
|a Prot�eines
|x Conformation.
|0 (CaQQLa)201-0217301
|
650 |
|
6 |
|a Prot�eines
|x Repliement.
|0 (CaQQLa)201-0217303
|
650 |
|
7 |
|a Protein folding.
|2 fast
|0 (OCoLC)fst01079687
|
650 |
|
7 |
|a Proteins
|x Conformation.
|2 fast
|0 (OCoLC)fst01079725
|
700 |
1 |
|
|a Wetzel, Ronald.
|
776 |
0 |
8 |
|i Print version:
|t Protein misassembly.
|d San Diego : Academic Press
|z 9780120342501
|w (OCoLC)37877105
|
830 |
|
0 |
|a Advances in protein chemistry ;
|v v. 50.
|
856 |
4 |
0 |
|u https://sciencedirect.uam.elogim.com/science/book/9780120342501
|z Texto completo
|